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Crystal structure of a heterotetrameric katanin p60:p80 complex
Faltova, L., Jiang, K., Frey, D., Wu, Y., Capitani, G., Prota, A. E., … Kammerer, R. A. (2019). Crystal structure of a heterotetrameric katanin p60:p80 complex. Structure, 27(9), 1375-1383.e3. https://doi.org/10.1016/j.str.2019.07.002
Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C
Benoit, R. M., Schärer, M. A., Wieser, M. M., Li, X., Frey, D., & Kammerer, R. A. (2017). Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C. Scientific Reports, 7, 43588 (7 pp.). https://doi.org/10.1038/srep43588
Structural basis for misregulation of kinesin KIF21A autoinhibition by CFEOM1 disease mutations
Bianchi, S., van Riel, W. E., Kraatz, S. H. W., Olieric, N., Frey, D., Katrukha, E. A., … Kammerer, R. A. (2016). Structural basis for misregulation of kinesin KIF21A autoinhibition by CFEOM1 disease mutations. Scientific Reports, 6, 30668 (16 pp.). https://doi.org/10.1038/srep30668
SAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architecture
Hilbert, M., Noga, A., Frey, D., Hamel, V., Guichard, P., Kraatz, S. H. W., … Steinmetz, M. O. (2016). SAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architecture. Nature Cell Biology, 18(4), 393-403. https://doi.org/10.1038/ncb3329
Centriolar CPAP/SAS-4 imparts slow processive microtubule growth
Sharma, A., Aher, A., Dynes, N. J., Frey, D., Katrukha, E. A., Jaussi, R., … Steinmetz, M. O. (2016). Centriolar CPAP/SAS-4 imparts slow processive microtubule growth. Developmental Cell, 37(4), 362-376. https://doi.org/10.1016/j.devcel.2016.04.024
Structure of the BoNT/A1 - Receptor complex
Benoit, R. M., Frey, D., Wieser, M. M., Thieltges, K. M., Jaussi, R., Capitani, G., & Kammerer, R. A. (2015). Structure of the BoNT/A1 - Receptor complex. Toxicon, 107(Part A), 25-31. https://doi.org/10.1016/j.toxicon.2015.08.002
Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A
Benoit, R. M., Frey, D., Hilbert, M., Kevenaar, J. T., Wieser, M. M., Stirnimann, C. U., … Kammerer, R. A. (2014). Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A. Nature, 505(7481), 108-111. https://doi.org/10.1038/nature12732
Coronin 1 regulates cognition and behavior through modulation of cAMP/Protein kinase A signaling
Jayachandran, R., Liu, X., BoseDasgupta, S., Müller, P., Zhang, C. L., Moshous, D., … Pieters, J. (2014). Coronin 1 regulates cognition and behavior through modulation of cAMP/Protein kinase A signaling. PLoS Biology, 12(3), e1001820 (21 pp.). https://doi.org/10.1371/journal.pbio.1001820
A type IV translocated Legionella cysteine phytase counteracts intracellular growth restriction by phytate
Weber, S., Stirnimann, C. U., Wieser, M., Frey, D., Meier, R., Engelhardt, S., … Hilbi, H. (2014). A type IV translocated Legionella cysteine phytase counteracts intracellular growth restriction by phytate. Journal of Biological Chemistry, 289(49), 34175-34188. https://doi.org/10.1074/jbc.M114.592568
Structural basis for the oligomerization-state switch from a dimer to a trimer of an engineered cortexillin-1 coiled-coil variant
Bjelić, S., Wieser, M., Frey, D., Stirnimann, C. U., Chance, M. R., Jaussi, R., … Kammerer, R. A. (2013). Structural basis for the oligomerization-state switch from a dimer to a trimer of an engineered cortexillin-1 coiled-coil variant. PLoS One, 8(5), e63370 (7 pp.). https://doi.org/10.1371/journal.pone.0063370
Structural basis of tubulin tyrosination by tubulin tyrosine ligase
Prota, A. E., Magiera, M. M., Kuijpers, M., Bargsten, K., Frey, D., Wieser, M., … Steinmetz, M. O. (2013). Structural basis of tubulin tyrosination by tubulin tyrosine ligase. Journal of Cell Biology, 200(3), 259-270. https://doi.org/10.1083/jcb.201211017
Interaction of mammalian end binding proteins with CAP-Gly domains of CLIP-170 and p150<sup>glued</sup>
Bjelić, S., De Groot, C. O., Schärer, M. A., Jaussi, R., Bargsten, K., Salzmann, M., … Steinmetz, M. O. (2012). Interaction of mammalian end binding proteins with CAP-Gly domains of CLIP-170 and p150glued. Journal of Structural Biology, 177(1), 160-167. https://doi.org/10.1016/j.jsb.2011.11.010
Automated seamless DNA co-transformation cloning with direct expression vectors applying positive or negative insert selection
Olieric, N., Kuchen, M., Wagen, S., Sauter, M., Crone, S., Edmondson, S., … Jaussi, R. (2010). Automated seamless DNA co-transformation cloning with direct expression vectors applying positive or negative insert selection. BMC Biotechnology, 10, 56. https://doi.org/10.1186/1472-6750-10-56
Automated unrestricted multigene recombineering for multiprotein complex production
Bieniossek, C., Nie, Y., Frey, D., Olieric, N., Schaffitzel, C., Collinson, I., … Berger, I. (2009). Automated unrestricted multigene recombineering for multiprotein complex production. Nature Methods, 6(6), 447-450. https://doi.org/10.1038/nmeth.1326
A genetically encoded photoactivatable Rac controls the motility of living cells
Wu, Y. I., Frey, D., Lungu, O. I., Jaehrig, A., Schlichting, I., Kuhlman, B., & Hahn, K. M. (2009). A genetically encoded photoactivatable Rac controls the motility of living cells. Nature, 461(7260), 104-108. https://doi.org/10.1038/nature08241
Structure of the recombinant antibody Fab fragment f3p4
Frey, D., Huber, T., Plückthun, A., & Grütter, M. G. (2008). Structure of the recombinant antibody Fab fragment f3p4. Acta Crystallographica Section D: Structural Biology, 64(6), 636-643. https://doi.org/10.1107/S0907444908007282
Production of in vitro amplified DNA pseudolibraries and high-throughput cDNA target amplification
Frey, D., Kambach, C., Steinmetz, M. O., & Jaussi, R. (2007). Production of in vitro amplified DNA pseudolibraries and high-throughput cDNA target amplification. BMC Biotechnology, 7, 31. https://doi.org/10.1186/1472-6750-7-31
Structure-function relationship of CAP-Gly domains
Weisbrich, A., Honnappa, S., Jaussi, R., Okhrimenko, O., Frey, D., Jelesarov, I., … Steinmetz, M. O. (2007). Structure-function relationship of CAP-Gly domains. Nature Structural and Molecular Biology, 14(10), 959-967. https://doi.org/10.1038/nsmb1291
Structure of the Mammalian NOS Regulator Dimethylarginine Dimethylaminohydrolase: A Basis for the Design of Specific Inhibitors
Frey, D., Braun, O., Briand, C., Vašák, M., & Grütter, M. G. (2006). Structure of the Mammalian NOS Regulator Dimethylarginine Dimethylaminohydrolase: A Basis for the Design of Specific Inhibitors. Structure, 14(5), 901-911. https://doi.org/10.1016/j.str.2006.03.006