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Volumn 92, Issue 12, 2007, Pages 4415-4423

Understanding ligand binding effects on the conformation of estrogen receptor α-DNA complexes: A combinational quartz crystal microbalance with dissipation and surface plasmon resonance study

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYTAMOXIFEN; DNA; ESTRADIOL; ESTROGEN RECEPTOR ALPHA;

EID: 34250323898     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.099382     Document Type: Article
Times cited : (77)

References (48)
  • 1
    • 33644638521 scopus 로고    scopus 로고
    • Estrogen receptors and human disease
    • Deroo, B. J., and K. S. Korach. 2006. Estrogen receptors and human disease. J. Clin. Invest. 116:561-570.
    • (2006) J. Clin. Invest , vol.116 , pp. 561-570
    • Deroo, B.J.1    Korach, K.S.2
  • 2
    • 0034237128 scopus 로고    scopus 로고
    • Neuroprotective effects of estrogen: Potential mechanisms of action
    • Green, P. S., and J. W. Simpkins. 2000. Neuroprotective effects of estrogen: potential mechanisms of action. Int. J. Devl. Neurosci. 18:347-358.
    • (2000) Int. J. Devl. Neurosci , vol.18 , pp. 347-358
    • Green, P.S.1    Simpkins, J.W.2
  • 3
    • 0031854357 scopus 로고    scopus 로고
    • Estrogen-mediated immunosupression in autoimmune diseases
    • Jansson, L., and R. Holmdahl. 1998. Estrogen-mediated immunosupression in autoimmune diseases. Inflamm. Res. 47:290-301.
    • (1998) Inflamm. Res , vol.47 , pp. 290-301
    • Jansson, L.1    Holmdahl, R.2
  • 4
    • 0033744048 scopus 로고    scopus 로고
    • Conformational changes and coactivator recruitment by novel ligands for estrogen receptor-α and estrogen receptor-β: Correlations with biological character and distinct differences among SRC coactivator family members
    • Kraichely, D. M., J. Sun, J. A. Katzenellenbogen, and B. S. Katzenellenbogen. 2000. Conformational changes and coactivator recruitment by novel ligands for estrogen receptor-α and estrogen receptor-β: correlations with biological character and distinct differences among SRC coactivator family members. Endocrinology. 141:3534-3545.
    • (2000) Endocrinology , vol.141 , pp. 3534-3545
    • Kraichely, D.M.1    Sun, J.2    Katzenellenbogen, J.A.3    Katzenellenbogen, B.S.4
  • 5
    • 0032230245 scopus 로고    scopus 로고
    • Interaction and dissociation by ligands of estrogen receptor and Hsp90: The antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm
    • Devin-Leclerc, J., X. Meng, F. Delahaye, P. Leclerc, E. Baulieu, and M. Catelli. 1998. Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm. Mol. Endocrinol. 12:842-854.
    • (1998) Mol. Endocrinol , vol.12 , pp. 842-854
    • Devin-Leclerc, J.1    Meng, X.2    Delahaye, F.3    Leclerc, P.4    Baulieu, E.5    Catelli, M.6
  • 6
    • 0028786569 scopus 로고
    • Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo
    • Wang, H., G. A. Peters, X. Zeng, M. Tang, W. Ip, and S. A. Khans. 1995. Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo. J. Biol. Chem. 270:23322-23329.
    • (1995) J. Biol. Chem , vol.270 , pp. 23322-23329
    • Wang, H.1    Peters, G.A.2    Zeng, X.3    Tang, M.4    Ip, W.5    Khans, S.A.6
  • 8
    • 0035878743 scopus 로고    scopus 로고
    • Estrogen receptor interaction with estrogen response elements
    • Klinge, C. M. 2001. Estrogen receptor interaction with estrogen response elements. Nucleic Acids Res. 29:2905-2919.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2905-2919
    • Klinge, C.M.1
  • 9
    • 0034595096 scopus 로고    scopus 로고
    • Estrogen receptors: How do they control reproductive and nonreproductive functions?
    • Muramatsu, M., and S. Inoue. 2000. Estrogen receptors: how do they control reproductive and nonreproductive functions? Biochem. Biophys. Res. Commun. 270:1-10.
    • (2000) Biochem. Biophys. Res. Commun , vol.270 , pp. 1-10
    • Muramatsu, M.1    Inoue, S.2
  • 10
    • 0034032022 scopus 로고    scopus 로고
    • Estrogen receptor interaction with co-activators and co-repressors
    • Klinge, C. M. 2000. Estrogen receptor interaction with co-activators and co-repressors. Steriods. 65:227-251.
    • (2000) Steriods , vol.65 , pp. 227-251
    • Klinge, C.M.1
  • 12
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau, A. K., D. Barstad, P. M. Loria, L. Cheng, P. J. Kushner, D. A. Agard, and G. L. Greene. 1998. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 95:927-937.
    • (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
  • 14
    • 0036213439 scopus 로고    scopus 로고
    • The effects of estrogen-responsive element- and ligand-induced structural changes on the recruitment of cofactors and transcriptional responses by ERα and ERβ
    • Yi, P., M. D. Driscoll, J. Huang, S. Bhagat, R. Hilf, R. A. Bambara, and M. Muyan. 2002. The effects of estrogen-responsive element- and ligand-induced structural changes on the recruitment of cofactors and transcriptional responses by ERα and ERβ. Mol. Endocrinol. 16:674-693.
    • (2002) Mol. Endocrinol , vol.16 , pp. 674-693
    • Yi, P.1    Driscoll, M.D.2    Huang, J.3    Bhagat, S.4    Hilf, R.5    Bambara, R.A.6    Muyan, M.7
  • 15
    • 0029044210 scopus 로고
    • Effect of antagonists on DNA binding properties of the human estrogen receptor in vitro and in vivo
    • Metzger, D., M. Berry, S. Ali, and P. Chambon. 1995. Effect of antagonists on DNA binding properties of the human estrogen receptor in vitro and in vivo. Mol. Endocrinol. 9:579-591.
    • (1995) Mol. Endocrinol , vol.9 , pp. 579-591
    • Metzger, D.1    Berry, M.2    Ali, S.3    Chambon, P.4
  • 16
    • 0031900850 scopus 로고    scopus 로고
    • Estrogen response elements function as allosteric modulators of estrogen receptor conformation
    • Wood, J. R., G. L. Greene, and A. M. Nardulli. 1998. Estrogen response elements function as allosteric modulators of estrogen receptor conformation. Mol. Cell. Biol. 18:1927-1934.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1927-1934
    • Wood, J.R.1    Greene, G.L.2    Nardulli, A.M.3
  • 17
    • 0034969440 scopus 로고    scopus 로고
    • Allosteric modulation of estrogen receptor conformation by different estrogen response elements
    • Wood, J. R., V. S. Likhite, M. A. Loven, and A. M. Nardulli. 2001. Allosteric modulation of estrogen receptor conformation by different estrogen response elements. Mol. Endocrinol. 15:1114-1126.
    • (2001) Mol. Endocrinol , vol.15 , pp. 1114-1126
    • Wood, J.R.1    Likhite, V.S.2    Loven, M.A.3    Nardulli, A.M.4
  • 18
    • 19444370062 scopus 로고    scopus 로고
    • The role of DNA response elements as allosteric modulators of steroid receptor function
    • Geserick, C., H. Meyer, and B. Haendler. 2005. The role of DNA response elements as allosteric modulators of steroid receptor function. Mol. Cell. Endocrinol. 236:1-7.
    • (2005) Mol. Cell. Endocrinol , vol.236 , pp. 1-7
    • Geserick, C.1    Meyer, H.2    Haendler, B.3
  • 19
    • 26444569477 scopus 로고    scopus 로고
    • Probing BSA binding to citrate-coated gold nanoparticles and surfaces
    • Brewer, S. H., W. R. Glomm, M. C. Johnson, M. K. Knag, and S. Franzen. 2005. Probing BSA binding to citrate-coated gold nanoparticles and surfaces. Langmuir. 21:9303-9307.
    • (2005) Langmuir , vol.21 , pp. 9303-9307
    • Brewer, S.H.1    Glomm, W.R.2    Johnson, M.C.3    Knag, M.K.4    Franzen, S.5
  • 20
    • 0032514637 scopus 로고    scopus 로고
    • Structural changes in hemoglobin during adsorption to solid surfaces: Effects of pH, ionic strength, and ligand binding
    • Höök, F., M. Rodahl, B. Kasemo, and P. Brzezinski. 1998. Structural changes in hemoglobin during adsorption to solid surfaces: effects of pH, ionic strength, and ligand binding. Proc. Natl. Acad. Sci. USA (Biophysics). 95:12271-12276.
    • (1998) Proc. Natl. Acad. Sci. USA (Biophysics) , vol.95 , pp. 12271-12276
    • Höök, F.1    Rodahl, M.2    Kasemo, B.3    Brzezinski, P.4
  • 21
    • 0035894177 scopus 로고    scopus 로고
    • Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: A quartz crystal microbalance with dissipation monitoring, ellipsometry, and surface plasmon resonance study
    • Höök, F., and B. Kasemo. 2001. Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: a quartz crystal microbalance with dissipation monitoring, ellipsometry, and surface plasmon resonance study. Anal. Chem. 73:5796-5804.
    • (2001) Anal. Chem , vol.73 , pp. 5796-5804
    • Höök, F.1    Kasemo, B.2
  • 22
    • 20444429099 scopus 로고    scopus 로고
    • Viscoelastic modeling of template-directed DNA synthesis
    • Stengel, G., F. Höök, and W. Knoll. 2005. Viscoelastic modeling of template-directed DNA synthesis. Anal. Chem. 77:3709-3714.
    • (2005) Anal. Chem , vol.77 , pp. 3709-3714
    • Stengel, G.1    Höök, F.2    Knoll, W.3
  • 23
    • 33746783462 scopus 로고    scopus 로고
    • Vesicle fusion studied by surface plasmon resonance and surface plasmon fluorescence spectroscopy
    • Morigaki, K., and K. Tawa. 2006. Vesicle fusion studied by surface plasmon resonance and surface plasmon fluorescence spectroscopy. Biophys. J. 91:1380-1387.
    • (2006) Biophys. J , vol.91 , pp. 1380-1387
    • Morigaki, K.1    Tawa, K.2
  • 24
    • 0041888238 scopus 로고    scopus 로고
    • In situ peptide-modified supported lipid bilayers for controlled cell attachment
    • Svedhem, S., D. Dahlborg, J. Ekeroth, J. Kelly, F. Hȯök, and J. Gold. 2003. In situ peptide-modified supported lipid bilayers for controlled cell attachment. Langmuir. 19:6730-6736.
    • (2003) Langmuir , vol.19 , pp. 6730-6736
    • Svedhem, S.1    Dahlborg, D.2    Ekeroth, J.3    Kelly, J.4    Hȯök, F.5    Gold, J.6
  • 26
    • 26944495690 scopus 로고    scopus 로고
    • Comparison of surface plasmon resonance spectroscopy and quartz crystal microbalance techniques for studying DNA assembly and hybridization
    • Su, X. D., Y. J. Wu, and W. Knoll. 2005. Comparison of surface plasmon resonance spectroscopy and quartz crystal microbalance techniques for studying DNA assembly and hybridization. Biosens. Bioelectron. 21:719-726.
    • (2005) Biosens. Bioelectron , vol.21 , pp. 719-726
    • Su, X.D.1    Wu, Y.J.2    Knoll, W.3
  • 27
    • 10644245241 scopus 로고    scopus 로고
    • Simultaneous surface plasmon resonance and quartz crystal microbalance with dissipation monitoring measurements of biomolecular adsorption events involving structural transformations and variations in coupled water
    • Reimhult, E., C. Larsson, B. Kasemo, and F. Höök. 2004. Simultaneous surface plasmon resonance and quartz crystal microbalance with dissipation monitoring measurements of biomolecular adsorption events involving structural transformations and variations in coupled water. Anal. Chem. 76:7211-7220.
    • (2004) Anal. Chem , vol.76 , pp. 7211-7220
    • Reimhult, E.1    Larsson, C.2    Kasemo, B.3    Höök, F.4
  • 28
    • 34250325895 scopus 로고    scopus 로고
    • QCM-D real-time monitoring of structural changes in an adsorbed protein layer
    • Application Notes:an41-an42
    • Zelander, G. 2006. QCM-D real-time monitoring of structural changes in an adsorbed protein layer. Nat. Methods. Application Notes:an41-an42.
    • (2006) Nat. Methods
    • Zelander, G.1
  • 29
    • 0024296177 scopus 로고    scopus 로고
    • A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor
    • Klein-Hitpass, L., G. U. Ryffel, E. Heitlinger, and A. B. C. Cato. 1998. A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor. Nucleic Acids Res. 16:647-663.
    • (1998) Nucleic Acids Res , vol.16 , pp. 647-663
    • Klein-Hitpass, L.1    Ryffel, G.U.2    Heitlinger, E.3    Cato, A.B.C.4
  • 30
    • 0347128041 scopus 로고    scopus 로고
    • Detection of point mutation and insertion mutations in DNA using a quartz crystal microbalance and MutS, a mismatch binding protein
    • Su, X. D., R. Robelek, Y. J. Wu, and W. Knoll. 2004. Detection of point mutation and insertion mutations in DNA using a quartz crystal microbalance and MutS, a mismatch binding protein. Anal. Chem. 76:489-494.
    • (2004) Anal. Chem , vol.76 , pp. 489-494
    • Su, X.D.1    Robelek, R.2    Wu, Y.J.3    Knoll, W.4
  • 31
    • 85030520426 scopus 로고    scopus 로고
    • User Manual for Autolab ESPRIT, Version 2. 2002. Chapter 7, p. 105.
    • User Manual for Autolab ESPRIT, Version 2. 2002. Chapter 7, p. 105.
  • 32
    • 0017858702 scopus 로고
    • Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface
    • de Feijter, J. A., J. Benjamins, and F. A. Veer. 1978. Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface. Biopolymers. 17:1759-1772.
    • (1978) Biopolymers , vol.17 , pp. 1759-1772
    • de Feijter, J.A.1    Benjamins, J.2    Veer, F.A.3
  • 33
    • 0032691940 scopus 로고    scopus 로고
    • Viscoelastic acoustic response of layered polymer films at fluid-solid interfaces: Continuum mechanics approach
    • Voinova, M. V., M. Rodahl, M. Jonson, and B. Kasemo. 1999. Viscoelastic acoustic response of layered polymer films at fluid-solid interfaces: continuum mechanics approach. Phys. Scr. 59:391-396.
    • (1999) Phys. Scr , vol.59 , pp. 391-396
    • Voinova, M.V.1    Rodahl, M.2    Jonson, M.3    Kasemo, B.4
  • 34
    • 0032000483 scopus 로고    scopus 로고
    • Energy dissipation kinetics for protein and antibody-antigen adsorption under shear oscillation on a quartz crystal microbalance
    • Höök, F., M. Rodahl, P. Brzezinski, and B. Kasemo. 1998. Energy dissipation kinetics for protein and antibody-antigen adsorption under shear oscillation on a quartz crystal microbalance. Langmuir. 14:729-734.
    • (1998) Langmuir , vol.14 , pp. 729-734
    • Höök, F.1    Rodahl, M.2    Brzezinski, P.3    Kasemo, B.4
  • 35
    • 3142694773 scopus 로고    scopus 로고
    • Human immunoglobin adsorption investigated by means of quartz crystal microbalance dissipation, atomic force microscopy and surface acoustic wave, and surface plasmon resonance techniques
    • Zhou, C., J. M. Friedt, A. Angelova, K. H. Choi, W. Laureyn, F. Frederix, L. A. Francis, A. Campitelli, Y. Engelborghs, and G. Borghs. 2004. Human immunoglobin adsorption investigated by means of quartz crystal microbalance dissipation, atomic force microscopy and surface acoustic wave, and surface plasmon resonance techniques. Langmuir. 20:5870-5878.
    • (2004) Langmuir , vol.20 , pp. 5870-5878
    • Zhou, C.1    Friedt, J.M.2    Angelova, A.3    Choi, K.H.4    Laureyn, W.5    Frederix, F.6    Francis, L.A.7    Campitelli, A.8    Engelborghs, Y.9    Borghs, G.10
  • 36
    • 0027141842 scopus 로고
    • DNA recognition by the oestrogen receptor: From solution to the crystal
    • Schwabe, J. W. R., L. C. Chapman, J. T. Finch, D. Rhodes, and D. Neuhaus. 1993. DNA recognition by the oestrogen receptor: from solution to the crystal. Structure. 15:187-204.
    • (1993) Structure , vol.15 , pp. 187-204
    • Schwabe, J.W.R.1    Chapman, L.C.2    Finch, J.T.3    Rhodes, D.4    Neuhaus, D.5
  • 37
    • 0035810957 scopus 로고    scopus 로고
    • Increase in the stability and helical content of estrogen receptor α in the presence of the estrogen response elements: Analysis by circular dichroism spectroscopy
    • Greenfield, N., V. Vijayanathan, T. J. Thomas, M. A. Gallo, and T. Thomas. 2001. Increase in the stability and helical content of estrogen receptor α in the presence of the estrogen response elements: analysis by circular dichroism spectroscopy. Biochemistry. 40:6646-6652.
    • (2001) Biochemistry , vol.40 , pp. 6646-6652
    • Greenfield, N.1    Vijayanathan, V.2    Thomas, T.J.3    Gallo, M.A.4    Thomas, T.5
  • 38
    • 0027462304 scopus 로고
    • Human estrogen receptor bound to an estrogen response element bends DNA
    • Nardulli, A. M., G. L. Greene, and D. J. Shapiro. 1993. Human estrogen receptor bound to an estrogen response element bends DNA. Mol. Endocrinol. 7:331-340.
    • (1993) Mol. Endocrinol , vol.7 , pp. 331-340
    • Nardulli, A.M.1    Greene, G.L.2    Shapiro, D.J.3
  • 39
    • 0026653078 scopus 로고
    • Estrogen receptor-induced bending of the Xenopus vitellogenin A2 gene hormone response element
    • Sabbah, M., S. L. Ricousse, G. Redeuilh, and E. E. Baulieu. 1992. Estrogen receptor-induced bending of the Xenopus vitellogenin A2 gene hormone response element. Biochem. Biophys. Res. Commun. 185:944-952.
    • (1992) Biochem. Biophys. Res. Commun , vol.185 , pp. 944-952
    • Sabbah, M.1    Ricousse, S.L.2    Redeuilh, G.3    Baulieu, E.E.4
  • 40
    • 33745757784 scopus 로고    scopus 로고
    • Molecular flexibility in protein-DNA interactions
    • Günther, S., K. Rother, and C. Frömmel. 2006. Molecular flexibility in protein-DNA interactions. Biosystems. 85:126-136.
    • (2006) Biosystems , vol.85 , pp. 126-136
    • Günther, S.1    Rother, K.2    Frömmel, C.3
  • 41
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and M. T. Jr. Record. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 44
    • 0030805890 scopus 로고    scopus 로고
    • Binding of the estrogen receptor to DNA. The role of waters
    • Kosztin, D., T. C. Bishop, and K. Schulten. 1997. Binding of the estrogen receptor to DNA. The role of waters. Biophys. J. 73:557-570.
    • (1997) Biophys. J , vol.73 , pp. 557-570
    • Kosztin, D.1    Bishop, T.C.2    Schulten, K.3
  • 45
    • 0036161285 scopus 로고    scopus 로고
    • A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and the quartz crystal microbalance/dissipation
    • Höök, M., J. Rodahl, R. Vörös, P. Kurrat, J. J. Böni, M. Ramsden, N. D. Textor, P. Spencer, J. Tengvall, B. Gold, and B. Kasemo. 2002. A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and the quartz crystal microbalance/dissipation. Colloids Surf. B Biointerfaces. 24:155-170.
    • (2002) Colloids Surf. B Biointerfaces , vol.24 , pp. 155-170
    • Höök, M.1    Rodahl, J.2    Vörös, R.3    Kurrat, P.4    Böni, J.J.5    Ramsden, M.6    Textor, N.D.7    Spencer, P.8    Tengvall, J.9    Gold, B.10    Kasemo, B.11
  • 46
    • 33847668930 scopus 로고    scopus 로고
    • Characterization of protein-DNA interactions using surface plasmon resonance spectroscopy with various assay schemes
    • Teh, H. F., W. Y. X. Peh, X. D. Su, and J. S. Thomsen. 2006. Characterization of protein-DNA interactions using surface plasmon resonance spectroscopy with various assay schemes. Biochemistry. 46:2127-2135.
    • (2006) Biochemistry , vol.46 , pp. 2127-2135
    • Teh, H.F.1    Peh, W.Y.X.2    Su, X.D.3    Thomsen, J.S.4
  • 47
    • 0034235830 scopus 로고    scopus 로고
    • Quantitative characterization of the interaction between purified human estrogen receptor α and DNA using fluorescence anisotropy
    • Boyer, M., N. Poujol, E. Margeat, and C. A. Royer. 2000. Quantitative characterization of the interaction between purified human estrogen receptor α and DNA using fluorescence anisotropy. Nucleic Acids Res. 28:2494-2502.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2494-2502
    • Boyer, M.1    Poujol, N.2    Margeat, E.3    Royer, C.A.4
  • 48
    • 0037423637 scopus 로고    scopus 로고
    • Ligands differentially modulate the protein interactions of the human estrogen receptors α and β
    • Margeat, E., A. Bourdoncle, R. Margueron, N. Poujol, V. Cavaillès, and C. A. Royer. 2003. Ligands differentially modulate the protein interactions of the human estrogen receptors α and β. J. Mol. Biol. 326:77-92.
    • (2003) J. Mol. Biol , vol.326 , pp. 77-92
    • Margeat, E.1    Bourdoncle, A.2    Margueron, R.3    Poujol, N.4    Cavaillès, V.5    Royer, C.A.6


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