Connection
David Bain to Dimerization
This is a "connection" page, showing publications David Bain has written about Dimerization.
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0.507 |
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Moody AD, Miura MT, Connaghan KD, Bain DL. Thermodynamic dissection of estrogen receptor-promoter interactions reveals that steroid receptors differentially partition their self-association and promoter binding energetics. Biochemistry. 2012 Jan 24; 51(3):739-49.
Score: 0.097
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Connaghan-Jones KD, Heneghan AF, Miura MT, Bain DL. 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. 2008 Apr 04; 377(4):1144-60.
Score: 0.074
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Heneghan AF, Connaghan-Jones KD, Miura MT, Bain DL. Coactivator assembly at the promoter: efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor. Biochemistry. 2007 Oct 02; 46(39):11023-32.
Score: 0.072
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Connaghan-Jones KD, Heneghan AF, Miura MT, Bain DL. Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function. Proc Natl Acad Sci U S A. 2007 Feb 13; 104(7):2187-92.
Score: 0.069
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Connaghan-Jones KD, Heneghan AF, Miura MT, Bain DL. Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range. Biochemistry. 2006 Oct 03; 45(39):12090-9.
Score: 0.068
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Heneghan AF, Connaghan-Jones KD, Miura MT, Bain DL. Cooperative DNA binding by the B-isoform of human progesterone receptor: thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly. Biochemistry. 2006 Mar 14; 45(10):3285-96.
Score: 0.065
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Heneghan AF, Berton N, Miura MT, Bain DL. Self-association energetics of an intact, full-length nuclear receptor: the B-isoform of human progesterone receptor dimerizes in the micromolar range. Biochemistry. 2005 Jul 12; 44(27):9528-37.
Score: 0.062