A high-throughput fluorescence-anisotropy screen that identifies small molecule inhibitors of the DNA binding of B-ZIP transcription factors.

@article{Rishi2005AHF,
  title={A high-throughput fluorescence-anisotropy screen that identifies small molecule inhibitors of the DNA binding of B-ZIP transcription factors.},
  author={Vikas Rishi and Timothy Potter and Julie Laudeman and Russel Reinhart and Thomas E. Silvers and Michael J. Selby and Timothy Stevenson and Paula M Krosky and Andrew G. Stephen and Asha Acharya and Jon Moll and Won Jun Oh and Dominic A. Scudiero and Robert H. Shoemaker and Charles Vinson},
  journal={Analytical biochemistry},
  year={2005},
  volume={340 2},
  pages={259-71}
}
We have developed a high-throughput fluorescence anisotropy screen, using a 384-well format, to identify small molecules that disrupt the DNA binding of B-ZIP proteins. Binding of a B-ZIP dimer to fluorescently labeled DNA can be monitored by fluorescence anisotropy. We screened the National Cancer Institute diversity set of 1990 compounds to identify small molecules that disrupt the B-ZIP|DNA complex of CREB, C/EBPbeta, VBP, and AP-1 (FOS|JUND) bound to their cognate DNA sequence. We… CONTINUE READING