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Tight and specific lanthanide binding in a de novo TIM barrel with a large internal cavity designed by symmetric domain fusion
Caldwell, S. J., Haydon, I. C., Piperidou, N., Huang, P. S., Bick, M. J., Sjöström, H. S., … Zeymer, C. (2020). Tight and specific lanthanide binding in a de novo TIM barrel with a large internal cavity designed by symmetric domain fusion. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(48), 30362-30369. https://doi.org/10.1073/pnas.2008535117
Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein
Mylemans, B., Noguchi, H., Deridder, E., Lescrinier, E., Tame, J. R. H., & Voet, A. R. D. (2020). Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein. Protein Science, 29(12), 2375-2386. https://doi.org/10.1002/pro.3961
An interface-driven design strategy yields a novel, corrugated protein architecture
ElGamacy, M., Coles, M., Ernst, P., Zhu, H., Hartmann, M. D., Plückthun, A., & Lupas, A. N. (2018). An interface-driven design strategy yields a novel, corrugated protein architecture. ACS Synthetic Biology, 7(9), 2226-2235. https://doi.org/10.1021/acssynbio.8b00224
DARPin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography
Batyuk, A., Wu, Y., Honegger, A., Heberling, M. M., & Plückthun, A. (2016). DARPin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography. Journal of Molecular Biology, 428(8), 1574-1588. https://doi.org/10.1016/j.jmb.2016.03.002
A designed conformational shift to control protein binding specificity
Michielssens, S., Peters, J. Henning, Ban, D., Pratihar, S., Seeliger, D., Sharma, M., … de Groot, B. L. (2014). A designed conformational shift to control protein binding specificity. Angewandte Chemie International Edition, 53(39), 10367-10371. https://doi.org/10.1002/anie.201403102
From DARPins to LoopDARPins: Novel LoopDARPin design allows the selection of low picomolar binders in a single round of ribosome display
Schilling, J., Schöppe, J., & Plückthun, A. (2014). From DARPins to LoopDARPins: Novel LoopDARPin design allows the selection of low picomolar binders in a single round of ribosome display. Journal of Molecular Biology, 426(3), 691-721. https://doi.org/10.1016/j.jmb.2013.10.026
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
What makes Ras an efficient molecular switch: A computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf
Filchtinski, D., Sharabi, O., Rüppel, A., Vetter, I. R., Herrmann, C., & Shifman, J. M. (2010). What makes Ras an efficient molecular switch: A computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf. Journal of Molecular Biology, 399(3), 422-435. https://doi.org/10.1016/j.jmb.2010.03.046
A βα-barrel built by the combination of fragments from different folds
Bharat, T. A. M., Eisenbeis, S., Zeth, K., & Höcker, B. (2008). A βα-barrel built by the combination of fragments from different folds. Proceedings of the National Academy of Sciences of the United States of America PNAS, 105(29), 9942-9947. https://doi.org/10.1073/pnas.0802202105
Crystal structure of a consensus-designed ankyrin repeat protein: Implications for stability
Binz, H. K., Kohl, A., Plückthun, A., & Grütter, M. G. (2006). Crystal structure of a consensus-designed ankyrin repeat protein: Implications for stability. Proteins, 65(2), 280-284. https://doi.org/10.1002/prot.20930