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Insulin binding to the analytical antibody sandwich pair OXI‐005 and HUI‐018: epitope mapping and binding properties
Johansson, E., Wu, X., Yu, B., Yang, Z., Cao, Z., Wiberg, C., … Poulsen, F. (2021). Insulin binding to the analytical antibody sandwich pair OXI‐005 and HUI‐018: epitope mapping and binding properties. Protein Science, 30(2), 485-496. https://doi.org/10.1002/pro.4009
Extension of a <em>de novo</em> TIM barrel with a rationally designed secondary structure element
Wiese, J. G., Shanmugaratnam, S., & Höcker, B. (2021). Extension of a de novo TIM barrel with a rationally designed secondary structure element. Protein Science. https://doi.org/10.1002/pro.4064
Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors
Bokhovchuk, F., Mesrouze, Y., Delaunay, C., Martin, T., Villard, F., Meyerhofer, M., … Chène, P. (2020). Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors. Protein Science, 29(2), 509-520. https://doi.org/10.1002/pro.3775
X-ray crystal structure localizes the mechanism of inhibition of an IL-36R antagonist monoclonal antibody to interaction with Ig1 and Ig2 extra cellular domains
Larson, E. T., Brennan, D. L., Hickey, E. R., Ganesan, R., Kroe‐Barrett, R., & Farrow, N. A. (2020). X-ray crystal structure localizes the mechanism of inhibition of an IL-36R antagonist monoclonal antibody to interaction with Ig1 and Ig2 extra cellular domains. Protein Science, 29(7), 1679-1686. https://doi.org/10.1002/pro.3862
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
Type I fatty acid synthase trapped in the octanoyl-bound state
Rittner, A., Paithankar, K. S., Himmler, A., & Grininger, M. (2020). Type I fatty acid synthase trapped in the octanoyl-bound state. Protein Science, 29(2), 589-605. https://doi.org/10.1002/pro.3797
Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface
Mesrouze, Y., Bokhovchuk, F., Izaac, A., Meyerhofer, M., Zimmermann, C., Fontana, P., … Chène, P. (2018). Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface. Protein Science, 27(10), 1810-1820. https://doi.org/10.1002/pro.3493
The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding
Dietrich, M. H., Harprecht, C., & Stehle, T. (2017). The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding. Protein Science, 26(12), 2342-2354. https://doi.org/10.1002/pro.3319
Structures of designed armadillo repeat proteins binding to peptides fused to globular domains
Hansen, S., Kiefer, J. D., Madhurantakam, C., Mittl, P. R. E., & Plückthun, A. (2017). Structures of designed armadillo repeat proteins binding to peptides fused to globular domains. Protein Science, 26(10), 1942-1952. https://doi.org/10.1002/pro.3229
Effect of the acylation of TEAD4 on its interaction with co-activators YAP and TAZ
Mesrouze, Y., Meyerhofer, M., Bokhovchuk, F., Fontana, P., Zimmermann, C., Martin, T., … Chène, P. (2017). Effect of the acylation of TEAD4 on its interaction with co-activators YAP and TAZ. Protein Science, 26(12), 2399-2409. https://doi.org/10.1002/pro.3312
Structure of the Y. pseudotuberculosis adhesin InvasinE
Sadana, P., Mönnich, M., Unverzagt, C., & Scrima, A. (2017). Structure of the Y. pseudotuberculosis adhesin InvasinE. Protein Science, 26(6), 1182-1195. https://doi.org/10.1002/pro.3171
The macro domain as fusion tag for carrier-driven crystallization
Wild, R., & Hothorn, M. (2017). The macro domain as fusion tag for carrier-driven crystallization. Protein Science, 26(2), 365-374. https://doi.org/10.1002/pro.3073
The impact of crystallization conditions on structure-based drug design: A case study on the methylene blue/acetylcholinesterase complex
Dym, O., Song, W., Felder, C., Roth, E., Shnyrov, V., Ashani, Y., … Silman, I. (2016). The impact of crystallization conditions on structure-based drug design: A case study on the methylene blue/acetylcholinesterase complex. Protein Science, 25(6), 1096-1114. https://doi.org/10.1002/pro.2923
Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus
Burchacka, E., Zdzalik, M., Niemczyk, J. S., Pustelny, K., Popowicz, G., Wladyka, B., … Oleksyszyn, J. (2014). Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus. Protein Science, 23(2), 179-189. https://doi.org/10.1002/pro.2403
A decade of crystallization drops: Crystallization of the cbb3 cytochrome c oxidase from Pseudomonas stutzeri
Buschmann, S., Richers, S., Ermler, U., & Michel, H. (2014). A decade of crystallization drops: Crystallization of the cbb3 cytochrome c oxidase from Pseudomonas stutzeri. Protein Science, 23(4), 411-422. https://doi.org/10.1002/pro.2423
Crystal structures of designed armadillo repeat proteins: Implications of construct design and crystallization conditions on overall structure
Reichen, C., Madhurantakam, C., Plückthun, A., & Mittl, P. R. E. (2014). Crystal structures of designed armadillo repeat proteins: Implications of construct design and crystallization conditions on overall structure. Protein Science, 23(11), 1572-1583. https://doi.org/10.1002/pro.2535
The three-dimensional structure of TrmB, a transcriptional regulator of dual function in the hyperthermophilic archaeon Pyrococcus furiosus in complex with sucrose
Krug, M., Lee, S. J., Boos, W., Diederichs, K., & Welte, W. (2013). The three-dimensional structure of TrmB, a transcriptional regulator of dual function in the hyperthermophilic archaeon Pyrococcus furiosus in complex with sucrose. Protein Science, 22(6), 800-808. https://doi.org/10.1002/pro.2263
Design, construction, and characterization of a second-generation DARPin library with reduced hydrophobicity
Seeger, M. A., Zbinden, R., Flütsch, A., Gutte, P. G. M., Engeler, S., Roschitzki-Voser, H., & Grütter, M. G. (2013). Design, construction, and characterization of a second-generation DARPin library with reduced hydrophobicity. Protein Science, 22(9), 1239-1257. https://doi.org/10.1002/pro.2312
Structure-based optimization of designed Armadillo-repeat proteins
Madhurantakam, C., Varadamsetty, G., Grütter, M. G., Plückthun, A., & Mittl, P. R. E. (2012). Structure-based optimization of designed Armadillo-repeat proteins. Protein Science, 21(7), 1015-1028. https://doi.org/10.1002/pro.2085
PLP-dependent enzymes as entry and exit gates of sphingolipid metabolism
Bourquin, F., Capitani, G., & Grütter, M. G. (2011). PLP-dependent enzymes as entry and exit gates of sphingolipid metabolism. Protein Science, 20(9), 1492-1508. https://doi.org/10.1002/pro.679