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Directed evolution of piperazic acid incorporation by a nonribosomal peptide synthetase**
Stephan, P., Langley, C., Winkler, D., Basquin, J., Caputi, L., O'Connor, S. E., & Kries, H. (2023). Directed evolution of piperazic acid incorporation by a nonribosomal peptide synthetase**. Angewandte Chemie International Edition, 62(35), e202304843 (6 pp.). https://doi.org/10.1002/anie.202304843
Crystal structure of CC chemokine receptor 2A in complex with an orthosteric antagonist provides insights for the design of selective antagonists
Apel, A. K., Cheng, R. K. Y., Tautermann, C. S., Brauchle, M., Huang, C. Y., Pautsch, A., … Schnapp, G. (2019). Crystal structure of CC chemokine receptor 2A in complex with an orthosteric antagonist provides insights for the design of selective antagonists. Structure, 27(3), 427-438.e5. https://doi.org/10.1016/j.str.2018.10.027
Curvature of designed armadillo repeat proteins allows modular peptide binding
Hansen, S., Ernst, P., König, S. L. B., Reichen, C., Ewald, C., Nettels, D., … Plückthun, A. (2018). Curvature of designed armadillo repeat proteins allows modular peptide binding. Journal of Structural Biology, 201(2), 108-117. https://doi.org/10.1016/j.jsb.2017.08.009
MoFvAb: Modeling the Fv region of antibodies
Bujotzek, A., Fuchs, A., Qu, C., Benz, J. O., Klostermann, S., Antes, I., & Georges, G. (2015). MoFvAb: Modeling the Fv region of antibodies. mAbs, 7(5), 838-852. https://doi.org/10.1080/19420862.2015.1068492
Hapten-directed spontaneous disulfide shuffling: a universal technology for site-directed covalent coupling of payloads to antibodies
Dengl, S., Hoffmann, E., Grote, M., Wagner, C., Mundigl, O., Georges, G., … Brinkmann, U. (2015). Hapten-directed spontaneous disulfide shuffling: a universal technology for site-directed covalent coupling of payloads to antibodies. FASEB Journal, 29(5), 1763-1779. https://doi.org/10.1096/fj.14-263665
Green-to-red photoconvertible dronpa mutant for multimodal super-resolution fluorescence microscopy
Moeyaert, B., Nguyen Bich, N., De Zitter, E., Rocha, S., Clays, K., Mizuno, H., … Dedecker, P. (2014). Green-to-red photoconvertible dronpa mutant for multimodal super-resolution fluorescence microscopy. ACS Nano, 8(2), 1664-1673. https://doi.org/10.1021/nn4060144
Change in protein-ligand specificity through binding pocket grafting
Scheib, U., Shanmugaratnam, S., Farías-Rico, J. A., & Höcker, B. (2014). Change in protein-ligand specificity through binding pocket grafting. Journal of Structural Biology, 185(2), 186-192. https://doi.org/10.1016/j.jsb.2013.06.002
Development of a generic adenovirus delivery system based on structure-guided design of bispecific trimeric DARPin adapters
Dreier, B., Honegger, A., Hess, C., Nagy-Davidescu, G., Mittl, P. R. E., Grütter, M. G., … Plückthun, A. (2013). Development of a generic adenovirus delivery system based on structure-guided design of bispecific trimeric DARPin adapters. Proceedings of the National Academy of Sciences of the United States of America PNAS, 110(10), E869-E877. https://doi.org/10.1073/pnas.1213653110
(4<em>R</em>)- and (4<em>S</em>)-fluoroproline in the conserved <em>cis</em>-prolyl peptide bond of the thioredoxin fold: tertiary structure context dictates ring puckering
Rubini, M., Schärer, M. A., Capitani, G., & Glockshuber, R. (2013). (4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold: tertiary structure context dictates ring puckering. ChemBioChem, 14(9), 1053-1057. https://doi.org/10.1002/cbic.201300178
Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein
Gaudry, A., Lorber, B., Neuenfeldt, A., Sauter, C., Florentz, C., & Sissler, M. (2012). Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein. Protein Engineering Design & Selection, 25(9), 473-481. https://doi.org/10.1093/protein/gzs046
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine
Aldag, C., Gromov, I. A., García-Rubio, I., von Koenig, K., Schlichting, I., Jaun, B., & Hilvert, D. (2009). Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine. Proceedings of the National Academy of Sciences of the United States of America PNAS, 106(14), 5481-5486. https://doi.org/10.1073/pnas.0810503106