Biblio

Found 20 results
Filters: Keyword is Drug Design and Author is Caflisch, A.  [Clear All Filters]
2019
Wiedmer L., Schärer C., Spiliotopoulos D., Hürzeler M., Śledź P., Caflisch A..  2019.  Ligand retargeting by binding site analogy. European Journal of Medicinal Chemistry. 175:107-113.
2018
Śledź P., Caflisch A..  2018.  Protein structure-based drug design: From docking to molecular dynamics. Current Opinion in Structural Biology. 48:93-102.
2017
Spiliotopoulos D., Zhu J., Wamhoff E.-C., Deerain N., Marchand J.-R., Aretz J., Rademacher C., Caflisch A..  2017.  Virtual screen to NMR (VS2NMR): Discovery of fragment hits for the CBP bromodomain. Bioorganic & Medicinal Chemistry Letters. 27(11):2472-2478.
2016
Unzue A., Xu M., Dong J., Wiedmer L., Spiliotopoulos D., Caflisch A., Nevado C..  2016.  Fragment-based design of selective nanomolar ligands of the CREBBP bromodomain. Journal of Medicinal Chemistry. 59(4):1350-1356.
Spiliotopoulos D., Caflisch A..  2016.  Fragment-based in silico screening of bromodomain ligands. Drug Discovery Today. Technologies. 19:81-90.
Unzue A., Lafleur K., Zhao H., Zhou T., Dong J., Kolb P., Liebl J., Zahler S., Caflisch A., Nevado C..  2016.  Three stories on Eph kinase inhibitors: From in silico discovery to in vivo validation. European Journal of Medicinal Chemistry. 112:347-366.
2015
Zhao H., Caflisch A..  2015.  Current kinase inhibitors cover a tiny fraction of fragment space. Bioorganic & Medicinal Chemistry Letters. 25(11):2372-2376.
Herrmann U.S, Schütz A.K, Shirani H., Huang D., Saban D., Nuvolone M., Li B., Ballmer B., Åslund A.KO, Mason J.J et al..  2015.  Structure-based drug design identifies polythiophenes as antiprion compounds. Science Translational Medicine. 7(299):299ra123.
2014
Pevzner Y., Frugier E., Schalk V., Caflisch A., Woodcock H.L.  2014.  Fragment-based docking: Development of the CHARMMing Web user interface as a platform for computer-aided drug design. Journal of Chemical Information and Modeling. 54(9):2612-2620.
Spiliotopoulos D., Caflisch A..  2014.  Molecular dynamics simulations of bromodomains reveal binding-site flexibility and multiple binding modes of the natural ligand acetyl-lysine. Israel Journal of Chemistry. 54(8-9):1084–1092.
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.
2012
Zhao H., Huang D., Caflisch A..  2012.  Discovery of tyrosine kinase inhibitors by docking into an inactive kinase conformation generated by molecular dynamics. ChemMedChem. 7(11):1983-1990.
2010
Zhou T., Caflisch A..  2010.  High-throughput virtual screening using quantum mechanical probes: Discovery of selective kinase inhibitors. ChemMedChem. 5(7):1007-1014.
Zhou T., Huang D., Caflisch A..  2010.  Quantum mechanical methods for drug design. Current Topics in Medicinal Chemistry. 10(1):33-45.
2005
Tartaglia G.G, Cavalli A., Pellarin R., Caflisch A..  2005.  Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Science. 14(10):2723-2734.
2001
Budin N., Ahmed S., Majeux N., Caflisch A..  2001.  An evolutionary approach for structure-based design of natural and non-natural peptidic ligands. Combinatorial Chemistry & High Throughput Screening. 4(8):661-673.
1999
Apostolakis J., Caflisch A..  1999.  Computational ligand design. Combinatorial Chemistry & High Throughput Screening. 2(2):91-104.
Majeux N., Scarsi M., Apostolakis J., Ehrhardt C., Caflisch A..  1999.  Exhaustive docking of molecular fragments with electrostatic solvation. Proteins: Structure, Function, and Bioinformatics. 37(1):88-105.
1996
Caflisch A..  1996.  Computational combinatorial ligand design: application to human α-thrombin. Journal of Computer-Aided Molecular Design. 10(5):372-396.
1993
Caflisch A., Miranker A., Karplus M..  1993.  Multiple copy simultaneous search and construction of ligands in binding sites: Application to inhibitors of HIV-1 aspartic proteinase. Journal of Medicinal Chemistry. 36(15):2142-2167.