메뉴 건너뛰기




Volumn 88, Issue 1, 2004, Pages 17-26

Molecular determinants of ERα and ERβ involved in selectivity of 16α-iodo-17β estradiol

Author keywords

16 Iodo 17 estradiol; ER ; ER ; Estradiol; Estrogen receptors; Molecular modeling

Indexed keywords

16ALPHA IODO 17BETA ESTRADIOL; ESTRADIOL DERIVATIVE; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 1542329067     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2003.10.009     Document Type: Article
Times cited : (11)

References (30)
  • 2
    • 0033304765 scopus 로고    scopus 로고
    • Estrogen actions in the central nervous system
    • McEwen B.S., Alves S.E. Estrogen actions in the central nervous system. Endocrine Rev. 20:1999;279-307.
    • (1999) Endocrine Rev. , vol.20 , pp. 279-307
    • McEwen, B.S.1    Alves, S.E.2
  • 6
    • 0030593681 scopus 로고    scopus 로고
    • ERβ: Identification and characterization of a novel human estrogen receptor
    • Mosselman S., Polman J., Dijkema R. ERβ: identification and characterization of a novel human estrogen receptor. FEBS Lett. 392:1996;49-53.
    • (1996) FEBS Lett. , vol.392 , pp. 49-53
    • Mosselman, S.1    Polman, J.2    Dijkema, R.3
  • 7
    • 0031790490 scopus 로고    scopus 로고
    • A novel human estrogen receptor β: Identification and functional analysis of additional N-terminal amino acids
    • Bhat R.A., Harnish D.C., Stevis P.E., Lyttle C.R., Komm B.S. A novel human estrogen receptor β: identification and functional analysis of additional N-terminal amino acids. J. Steroid. Biochem. Molec. Biol. 67:1998;233-240.
    • (1998) J. Steroid. Biochem. Molec. Biol. , vol.67 , pp. 233-240
    • Bhat, R.A.1    Harnish, D.C.2    Stevis, P.E.3    Lyttle, C.R.4    Komm, B.S.5
  • 8
    • 0025062215 scopus 로고
    • Role of the two activating domain of the estrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-estrogen 4 hydroxytamoxifene
    • Berry M., Metzer D., Chamboon P. Role of the two activating domain of the estrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-estrogen 4 hydroxytamoxifene. EMBO J. 9:1990;28112-28118.
    • (1990) EMBO J. , vol.9 , pp. 28112-28118
    • Berry, M.1    Metzer, D.2    Chamboon, P.3
  • 9
    • 84995870933 scopus 로고
    • Human estrogen receptor transactivation capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions
    • Tzukerman M.T., Esty A., Santiso-Mere D., Danielian P., Parker M.G., Stein R.B., Pike J.W., Mcdonnell D.P. Human estrogen receptor transactivation capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol. Endocrinol. 8:1994;21-30.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 21-30
    • Tzukerman, M.T.1    Esty, A.2    Santiso-Mere, D.3    Danielian, P.4    Parker, M.G.5    Stein, R.B.6    Pike, J.W.7    McDonnell, D.P.8
  • 10
    • 0031059270 scopus 로고    scopus 로고
    • The estradiol pharmacophore: Ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site
    • Anstead G.M., Carlson K.E., Katzenellenbogen J.A. The estradiol pharmacophore: ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site. Steroids. 62:1997;268-303.
    • (1997) Steroids , vol.62 , pp. 268-303
    • Anstead, G.M.1    Carlson, K.E.2    Katzenellenbogen, J.A.3
  • 11
    • 0029807308 scopus 로고    scopus 로고
    • Identification of amino acids in the hormone binding domain of the human estrogen receptor important in estrogen binding
    • Ekena K., Weis K.E., Katzenellenbogen J.A., Katzenellenbogen B.S. Identification of amino acids in the hormone binding domain of the human estrogen receptor important in estrogen binding. J. Biol. Chem. 271:1996;20053-20059.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20053-20059
    • Ekena, K.1    Weis, K.E.2    Katzenellenbogen, J.A.3    Katzenellenbogen, B.S.4
  • 12
    • 0031040614 scopus 로고    scopus 로고
    • Different residues of the human estrogen receptor are involved in the recognition of structurally diverse estrogens and antiestrogens
    • Ekena K., Weis K.E., Katzenellenbogen J.A., Katzenellenbogen B.S. Different residues of the human estrogen receptor are involved in the recognition of structurally diverse estrogens and antiestrogens. J. Biol. Chem. 272:1997;5069-5075.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5069-5075
    • Ekena, K.1    Weis, K.E.2    Katzenellenbogen, J.A.3    Katzenellenbogen, B.S.4
  • 14
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recogniotion and the antagonism of this interaction by tamoxifen
    • Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L. The structural basis of estrogen receptor/coactivator recogniotion and the antagonism of this interaction by tamoxifen. Cell. 95:1998;927-937.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 16
    • 0004752110 scopus 로고    scopus 로고
    • Novel ligands that function as selective estrogens or antiestrogens for estrogen receptor-α or estrogen receptor-β
    • Sun J., Meyers M.J., Fink B.E., Rajendran R., Katzenellenbogen J.A., Katzenellenbogen B.S. Novel ligands that function as selective estrogens or antiestrogens for estrogen receptor-α or estrogen receptor-β Endocrinology. 140:1999;800-804.
    • (1999) Endocrinology , vol.140 , pp. 800-804
    • Sun, J.1    Meyers, M.J.2    Fink, B.E.3    Rajendran, R.4    Katzenellenbogen, J.A.5    Katzenellenbogen, B.S.6
  • 19
    • 0036828135 scopus 로고    scopus 로고
    • Characterization of the biological roles of the estrogen receptors, ERα and ERβ, in estrogen target tissues in vivo through the use of ERα-selective ligand
    • Harris H.A., Katzenellenbogen J.A., Katzenellenbogen B.S. Characterization of the biological roles of the estrogen receptors, ERα and ERβ, in estrogen target tissues in vivo through the use of ERα-selective ligand. Endocrinology. 143:2002;4172-4177.
    • (2002) Endocrinology , vol.143 , pp. 4172-4177
    • Harris, H.A.1    Katzenellenbogen, J.A.2    Katzenellenbogen, B.S.3
  • 20
    • 0037312834 scopus 로고    scopus 로고
    • Molecular basis for the subtype discrimination of the estrogen receptor-β-selective ligand diarylpropionitrile
    • Sun J., Baudry J., Katzenellenbogen J.A., Katzenellenbogen B.S. Molecular basis for the subtype discrimination of the estrogen receptor-β-selective ligand diarylpropionitrile. Mol. Endocrinol. 17:2003;247-258.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 247-258
    • Sun, J.1    Baudry, J.2    Katzenellenbogen, J.A.3    Katzenellenbogen, B.S.4
  • 23
    • 0033279963 scopus 로고    scopus 로고
    • Biologically active estrogen receptor-β: Evidence from in vivo autoradiographic studies with estrogen receptor α-knockout mice
    • Shughrue P.J., Lane M.V., Merchenthaler I. Biologically active estrogen receptor-β: evidence from in vivo autoradiographic studies with estrogen receptor α-knockout mice. Endocrinology. 140:1999;2613-2620.
    • (1999) Endocrinology , vol.140 , pp. 2613-2620
    • Shughrue, P.J.1    Lane, M.V.2    Merchenthaler, I.3
  • 24
    • 0030848592 scopus 로고    scopus 로고
    • Characterization of bacterially expressed rat estrogen receptor β ligand binding domain by mass spectrometry: Structural comparison with estrogen receptor α
    • Witkowska H.E., Carlquist M., Engstrom O., Carlsson B., Bonn T., Gustafsson J.-A., Shackleton C.H.L. Characterization of bacterially expressed rat estrogen receptor β ligand binding domain by mass spectrometry: structural comparison with estrogen receptor α Steroids. 62:1997;621-631.
    • (1997) Steroids , vol.62 , pp. 621-631
    • Witkowska, H.E.1    Carlquist, M.2    Engstrom, O.3    Carlsson, B.4    Bonn, T.5    Gustafsson, J.-A.6    Shackleton, C.H.L.7
  • 25
    • 0036189788 scopus 로고    scopus 로고
    • The ligand binding profiles of estrogen receptors α and β are species dependent
    • Harris H.A., Bapat A.R., Gonder D.S., Frail D.E. The ligand binding profiles of estrogen receptors α and β are species dependent. Steroids. 67:2002;379-384.
    • (2002) Steroids , vol.67 , pp. 379-384
    • Harris, H.A.1    Bapat, A.R.2    Gonder, D.S.3    Frail, D.E.4
  • 26
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • Levitt M. Accurate modeling of protein conformation by automatic segment matching. J. Mol. Biol. 226:1992;507-533.
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 27
    • 1542336826 scopus 로고    scopus 로고
    • Computational approaches to understand selectivity between estrogen receptors alpha and beta
    • New York, NY, 2003, Abs COMP-248.
    • R.J. Unwalla, E.S. Manas, C. Miller, Zb. Xu, Computational approaches to understand selectivity between estrogen receptors alpha and beta. 226 ACS National Meeting, New York, NY, 2003, Abs COMP-248.
    • 226 ACS National Meeting
    • Unwalla, R.J.1    Manas, E.S.2    Miller, C.3    Xu, Zb.4
  • 28
    • 0031181346 scopus 로고    scopus 로고
    • QXP: Powerful, rapid computer algorithms for structure-based drug design
    • McMartin C., Bohacek R.S. QXP: powerful, rapid computer algorithms for structure-based drug design. J. Comput. Aided Mol. Des. 11:1997;333-344.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 333-344
    • McMartin, C.1    Bohacek, R.S.2
  • 30
    • 0038485612 scopus 로고    scopus 로고
    • Molecular determinants of the stereoselectivity of agonist activity of estrogen receptors (ER) α and β
    • Mueller S.O., Hall J.M., Swope D.L., Pedersen L.C., Korach K.S. Molecular determinants of the stereoselectivity of agonist activity of estrogen receptors (ER) α and β J. Biol. Chem. 278:2003;12255-12262.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12255-12262
    • Mueller, S.O.1    Hall, J.M.2    Swope, D.L.3    Pedersen, L.C.4    Korach, K.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.