Found 291 results
Filters: Author is Caflisch, A.  [Clear All Filters]
Müller C.S, Knehans T., Davydov D.R, Bounds P.L, von Mandach U., Halpert J.R, Caflisch A., Koppenol W.H.  2016.  Correction to "Concurrent cooperativity and substrate inhibition in the epoxidation of carbamazepine by cytochrome P450 3A4 active site mutants inspired by molecular dynamics simulations". Biochemistry. 55(39):5647.
Meyer P.A, Socias S., Key J., Ransey E., Tjon E.C, Buschiazzo A., Lei M., Botka C., Withrow J., Neau D. et al..  2016.  Data publication with the structural biology data grid supports live analysis. Nature Communications. 7:10882.
Marchand J.-R., Lolli G., Caflisch A..  2016.  Derivatives of 3-amino-2-methylpyridine as BAZ2B bromodomain ligands: In silico discovery and in crystallo validation. Journal of Medicinal Chemistry. 59(21):9919-9927.
Xu M., Unzue A., Dong J., Spiliotopoulos D., Nevado C., Caflisch A..  2016.  Discovery of CREBBP bromodomain inhibitors by high-throughput docking and hit optimization guided by molecular dynamics. Journal of Medicinal Chemistry. 59(4):1340-1349.
Arnon Z.A, Vitalis A., Levin A., Michaels T.CT, Caflisch A., Knowles T.PJ, Adler-Abramovich L., Gazit E..  2016.  Dynamic Microfluidic Control of Supramolecular Peptide Self-Assembly. Nature Communications. 7:13190.
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., Zhao H., Lolli G., Dong J., Zhu J., Zechner M., Dolbois A., Caflisch A., Nevado C..  2016.  The "gatekeeper" residue influences the mode of binding of acetyl indoles to bromodomains. Journal of Medicinal Chemistry. 59(7):3087-3097.
Lolli G., Caflisch A..  2016.  High-throughput fragment docking into the BAZ2B bromodomain: Efficient in silico screening for X-Ray crystallography. ACS Chemical Biology. 11(3):800-807.
Xu M., Caflisch A., Hamm P..  2016.  Protein structural memory influences ligand binding mode(s) and unbinding rates. Journal of Chemical Theory and Computation. 12(3):1393-1399.
Roos M., Pradère U., Ngondo R.P, Behera A., Allegrini S., Civenni G., Zagalak J.A, Marchand J.-R., Menzi M., Towbin H. et al..  2016.  A small-molecule inhibitor of Lin28. ACS Chemical Biology. 11(10):2773-2781.
Ben Halima S., Mishra S., Raja K.MP, Willem M., Baici A., Simons K., Brüstle O., Koch P., Haass C., Caflisch A. et al..  2016.  Specific inhibition of β-secretase processing of the Alzheimer disease amyloid precursor protein. Cell Reports. 14(9):2127-2141.
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.
Zhu J., Caflisch A..  2016.  Twenty crystal structures of bromodomain and PHD finger containing protein 1 (BRPF1)/ligand complexes reveal conserved binding motifs and rare interactions. Journal of Medicinal Chemistry. 59(11):5555-5561.
Marchand J.-R., Caflisch A..  2015.  Binding mode of acetylated histones to bromodomains: Variations on a common motif. ChemMedChem. 10(8):1327-1333.
Ewald C., Christen M.T, Watson R.P, Mihajlovic M., Zhou T., Honegger A., Plückthun A., Caflisch A., Zerbe O..  2015.  A combined NMR and computational approach to investigate Peptide binding to a designed armadillo repeat protein. Journal of Molecular Biology. 427(10):1916-1933.
Müller C.S, Knehans T., Davydov D.R, Bounds P.L, von Mandach U., Halpert J.R, Caflisch A., Koppenol W.H.  2015.  Concurrent cooperativity and substrate inhibition in the epoxidation of carbamazepine by cytochrome P450 3A4 active site mutants inspired by molecular dynamics simulations. Biochemistry. 54(3):711-721.
Zhao H., Caflisch A..  2015.  Current kinase inhibitors cover a tiny fraction of fragment space. Bioorganic & Medicinal Chemistry Letters. 25(11):2372-2376.
Huang D., Caflisch A..  2015.  Evolutionary conserved Tyr169 stabilizes the β2-α2 loop of the prion protein. Journal of the American Chemical Society. 137(8):2948-2957.
Zhao H., Caflisch A..  2015.  Molecular dynamics in drug design. European Journal of Medicinal Chemistry. 91:4-14.
Bacci M., Vitalis A., Caflisch A..  2015.  A molecular simulation protocol to avoid sampling redundancy and discover new states. Biochimica et Biophysica Acta (BBA) - General Subjects. 1850(5):889-902.
Blöchliger N., Xu M., Caflisch A..  2015.  Peptide binding to a PDZ domain by electrostatic steering via nonnative salt bridges. Biophysical Journal. 108(9):2362-2370.
Huang D., Caflisch A..  2015.  The roles of the conserved tyrosine in the β2-α2 loop of the prion protein. Prion. 9(6):412-419.
Dong J., Zhao H., Zhou T., Spiliotopoulos D., Rajendran C., Li X.-D., Huang D., Caflisch A..  2015.  Structural analysis of the binding of type I, I1/2, and II inhibitors to eph tyrosine kinases. ACS Medicinal Chemistry Letters. 6(1):79-83.
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.