@article{bibcite_159,
  keywords = {Models, Molecular, Animals, Structure-Activity Relationship, Aspartic Acid Endopeptidases, Binding Sites, Amyloid Precursor Protein Secretases, Endopeptidases, Static Electricity, Carbanilides, Cell Line, Cell Membrane Permeability, Databases, Factual, Fluorescence Resonance Energy Transfer, Mammals, Phenylurea Compounds, Thiadiazoles},
  author = {D. Huang and U. L{\"u}thi and P. Kolb and K. Edler and M. Cecchini and S. Audetat and A. Barberis and A. Caflisch},
  title = {Discovery of cell-permeable non-peptide inhibitors of beta-secretase by high-throughput docking and continuum electrostatics calculations},
  abstract = {<p>A fragment-based docking procedure followed by substructure search were used to identify active-site \&beta;-secretase inhibitors from a composite set of about 300 000 and a library of nearly 180 000 small molecules, respectively. EC<sub>50</sub> values less than 10 \&mu;M were measured in at least one of two different mammalian cell-based assays for 12 of the 72 purchased compounds. In particular, the phenylureathiadiazole 2 and the diphenylurea derivative 3 are promising lead compounds for \&beta;-secretase inhibition.</p>},
  year = {2005},
  journal = {Journal of Medicinal Chemistry},
  volume = {48},
  pages = {5108-5111},
  month = {2005 Aug 11},
  issn = {0022-2623},
  doi = {10.1021/jm050499d},
  language = {eng},
}