Structural interpretation of DNA–protein hydroxyl-radical footprinting experiments with high resolution using HYDROID
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology
Link
http://www.nature.com/articles/s41596-018-0048-z.pdf
Reference45 articles.
1. Tullius, T. D. Physical studies of protein-DNA complexes by footprinting. Annu. Rev. Biophys. Biophys. Chem. 18, 213–237 (1989).
2. Adilakshmi, T., Lease, R. A. & Woodson, S. A. Hydroxyl radical footprinting in vivo: mapping macromolecular structures with synchrotron radiation. Nucleic Acids Res. 34, e64 (2006).
3. Song, L. & Crawford, G. E. DNase-seq: a high-resolution technique for mapping active gene regulatory elements across the genome from mammalian cells. Cold Spring Harb. Protoc. https://doi.org/10.1101/pdb.prot5384 (2010).
4. Koohy, H., Down, T. A. & Hubbard, T. J. Chromatin accessibility data sets show bias due to sequence specificity of the DNase I enzyme. PLoS ONE 8, e69853 (2013).
5. Jain, S. S. & Tullius, T. D. Footprinting protein-DNA complexes using the hydroxyl radical. Nat. Protoc. 3, 1092–1100 (2008).
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