Connaghan, Keith D; Miura, Michael T; Maluf, Nasib K et al. (2013) Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic control. Biophys Chem 172:8-17
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Moody, Amie D; Robblee, James P; Bain, David L (2012) Dissecting the linkage between transcription factor self-assembly and site-specific DNA binding: the role of the analytical ultracentrifuge. Methods Mol Biol 796:187-204
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Bain, David L; Yang, Qin; Connaghan, Keith D et al. (2012) Glucocorticoid receptor-DNA interactions: binding energetics are the primary determinant of sequence-specific transcriptional activity. J Mol Biol 422:18-32
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Robblee, James P; Miura, Michael T; Bain, David L (2012) Glucocorticoid receptor-promoter interactions: energetic dissection suggests a framework for the specificity of steroid receptor-mediated gene regulation. Biochemistry 51:4463-72
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Moody, Amie D; Miura, Michael T; Connaghan, Keith D et al. (2012) Thermodynamic dissection of estrogen receptor-promoter interactions reveals that steroid receptors differentially partition their self-association and promoter binding energetics. Biochemistry 51:739-49
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Connaghan, Keith D; Moody, Amie D; Robblee, James P et al. (2011) From steroid receptors to cytokines: the thermodynamics of self-associating systems. Biophys Chem 159:24-32
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Connaghan, Keith D; Heneghan, Aaron F; Miura, Michael T et al. (2010) Na(+) and K(+) allosterically regulate cooperative DNA binding by the human progesterone receptor. Biochemistry 49:422-31
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Connaghan-Jones, Keith D; Bain, David L (2009) Using thermodynamics to understand progesterone receptor function: method and theory. Methods Enzymol 455:41-70
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Connaghan-Jones, Keith D; Heneghan, Aaron F; Miura, Michael T et al. (2008) Thermodynamic dissection of progesterone receptor interactions at the mouse mammary tumor virus promoter: monomer binding and strong cooperativity dominate the assembly reaction. J Mol Biol 377:1144-60
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Connaghan-Jones, Keith D; Moody, Amie D; Bain, David L (2008) Quantitative DNase footprint titration: a tool for analyzing the energetics of protein-DNA interactions. Nat Protoc 3:900-14
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