Lafleur, K., Dong, J., Huang, D., Caflisch, A., & Nevado, C. (2013). Optimization of inhibitors of the tyrosine kinase EphB4. 2. Cellular potency improvement and binding mode validation by X-ray crystallography. Journal of Medicinal Chemistry, 56(1), 84-96. https://doi.org/10.1021/jm301187e (Original work published)

Zhou, T., & Caflisch, A. (2010). High-throughput virtual screening using quantum mechanical probes: Discovery of selective kinase inhibitors. ChemMedChem, 5(7), 1007-1014. https://doi.org/10.1002/cmdc.201000085 (Original work published)

Huang, D., & Caflisch, A. (2010). Library screening by fragment-based docking. Journal of Molecular Recognition, 23(2), 183-193. https://doi.org/10.1002/jmr.981 (Original work published 2010)

Lafleur, K., Huang, D., Zhou, T., Caflisch, A., & Nevado, C. (2009). Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). Journal of Medicinal Chemistry, 52(20), 6433-6446. https://doi.org/10.1021/jm9009444 (Original work published)

Kolb, P., Kipouros, C. B., Huang, D., & Caflisch, A. (2008). Structure-based tailoring of compound libraries for high-throughput screening: Discovery of novel EphB4 kinase inhibitors. Proteins: Structure, Function, and Bioinformatics, 73(1), 11-18. https://doi.org/10.1002/prot.22028 (Original work published 2008)

Kolb, P., & Caflisch, A. (2006). Automatic and efficient decomposition of two-dimensional structures of small molecules for fragment-based high-throughput docking. Journal of Medicinal Chemistry, 49(25), 7384-7392. https://doi.org/10.1021/jm060838i (Original work published)

Unzue, A., Dong, J., Lafleur, K., Zhao, H., Frugier, E., Caflisch, A., & Nevado, C. (2014). Pyrrolo[3,2-b]quinoxaline derivatives as types I1/2 and II Eph tyrosine kinase inhibitors: Structure-based design, synthesis, and in vivo validation. Journal of Medicinal Chemistry, 57(15), 6834-6844. https://doi.org/10.1021/jm5009242 (Original work published)