Published in Nat Protoc on January 01, 2008
An ancient protein-DNA interaction underlying metazoan sex determination. Nat Struct Mol Biol (2015) 0.98
Progestin regulated miRNAs that mediate progesterone receptor action in breast cancer. Mol Cell Endocrinol (2012) 0.92
Glucocorticoid receptor-promoter interactions: energetic dissection suggests a framework for the specificity of steroid receptor-mediated gene regulation. Biochemistry (2012) 0.91
Quantitative detection of small molecule/DNA complexes employing a force-based and label-free DNA-microarray. Biophys J (2009) 0.87
Thermodynamic dissection of estrogen receptor-promoter interactions reveals that steroid receptors differentially partition their self-association and promoter binding energetics. Biochemistry (2012) 0.83
Single-molecule kinetics and footprinting of DNA bis-intercalation: the paradigmatic case of Thiocoraline. Nucleic Acids Res (2015) 0.81
Dissection of androgen receptor-promoter interactions: steroid receptors partition their interaction energetics in parallel with their phylogenetic divergence. J Mol Biol (2013) 0.78
Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic control. Biophys Chem (2012) 0.77
Steroid receptor-DNA interactions: toward a quantitative connection between energetics and transcriptional regulation. Nucleic Acids Res (2013) 0.76
Trimeric structure for an essential protein in L1 retrotransposition. Proc Natl Acad Sci U S A (2003) 1.43
Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range. Biochemistry (2006) 0.98
Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function. Proc Natl Acad Sci U S A (2007) 0.98
Coactivator assembly at the promoter: efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor. Biochemistry (2007) 0.97
Cooperative DNA binding by the B-isoform of human progesterone receptor: thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly. Biochemistry (2006) 0.95
Self-association energetics of an intact, full-length nuclear receptor: the B-isoform of human progesterone receptor dimerizes in the micromolar range. Biochemistry (2005) 0.95
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) 0.93
Glucocorticoid receptor-promoter interactions: energetic dissection suggests a framework for the specificity of steroid receptor-mediated gene regulation. Biochemistry (2012) 0.91
Structural and conformational analysis of the oxidase to dehydrogenase conversion of xanthine oxidoreductase. J Biol Chem (2002) 0.89
Functional properties of the N-terminal region of progesterone receptors and their mechanistic relationship to structure. J Steroid Biochem Mol Biol (2003) 0.85
Thermodynamic dissection of estrogen receptor-promoter interactions reveals that steroid receptors differentially partition their self-association and promoter binding energetics. Biochemistry (2012) 0.83
Oxidation and nuclear localization of thioredoxin-1 in sparse cell cultures. J Cell Biochem (2008) 0.82
Na(+) and K(+) allosterically regulate cooperative DNA binding by the human progesterone receptor. Biochemistry (2010) 0.81
Dissection of androgen receptor-promoter interactions: steroid receptors partition their interaction energetics in parallel with their phylogenetic divergence. J Mol Biol (2013) 0.78
Using thermodynamics to understand progesterone receptor function: method and theory. Methods Enzymol (2009) 0.77
Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic control. Biophys Chem (2012) 0.77
From steroid receptors to cytokines: the thermodynamics of self-associating systems. Biophys Chem (2011) 0.75
Dissecting the linkage between transcription factor self-assembly and site-specific DNA binding: the role of the analytical ultracentrifuge. Methods Mol Biol (2012) 0.75
Homologous steroid receptors assemble at identical promoter architectures with unique energetics of cooperativity. Proteins (2014) 0.75