@article{bibcite_466,
  keywords = {Computer Simulation, Drug Design, Humans, Ligands, Nuclear Proteins, Small Molecule Libraries, CREB-Binding Protein, Transcription Factors, Protein Domains},
  author = {D. Spiliotopoulos and A. Caflisch},
  title = {Fragment-based in silico screening of bromodomain ligands},
  abstract = {<p>We review the results of fragment-based high-throughput docking to the N-terminal bromodomain of BRD4 and the CREBBP bromodomain. In both docking campaigns the ALTA (anchor-based library tailoring) procedure was used to reduce the size of the initial library by selecting for flexible docking only the molecules that contain a fragment with favorable predicted binding energy. Ranking by a force field-based energy with solvation has resulted in small-molecule hits with low-micromolar affinity and favorable ligand efficiency. Importantly, the binding modes predicted by docking have been validated by X-ray crystallography. One of the hits for the CREBBP bromodomain has been optimized by medicinal chemistry into a series of potent and selective ligands.</p>},
  year = {2016},
  journal = {Drug Discovery Today. Technologies},
  volume = {19},
  chapter = {81},
  pages = {81-90},
  month = {2016 Mar},
  issn = {1740-6749},
  doi = {10.1016/j.ddtec.2016.06.003},
  language = {eng},
}