| Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten
Christen, P., Jaussi, R., & Benoit, R. (2024). Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten (2nd ed.). https://doi.org/10.1007/978-3-662-65477-4 |
| Development of radiofluorinated MLN-4760 derivatives for PET imaging of the SARS-CoV-2 entry receptor ACE2
Wang, J., Beyer, D., Vaccarin, C., He, Y., Tanriver, M., Benoit, R., … Müller, C. (2024). Development of radiofluorinated MLN-4760 derivatives for PET imaging of the SARS-CoV-2 entry receptor ACE2. European Journal of Nuclear Medicine and Molecular Imaging. https://doi.org/10.1007/s00259-024-06831-6 |
| OligoBinders: bioengineered soluble amyloid-like nanoparticles to bind and neutralize SARS-CoV-2
Behbahanipour, M., Benoit, R., Navarro, S., & Ventura, S. (2023). OligoBinders: bioengineered soluble amyloid-like nanoparticles to bind and neutralize SARS-CoV-2. ACS Applied Materials and Interfaces, 15(9), 11444-11457. https://doi.org/10.1021/acsami.2c18305 |
| Semisynthetic LC3 probes for autophagy pathways reveal a noncanonical LC3 interacting region motif crucial for the enzymatic activity of human ATG3
Farnung, J., Muhar, M., Liang, J. R., Tolmachova, K. A., Benoit, R. M., Corn, J. E., & Bode, J. W. (2023). Semisynthetic LC3 probes for autophagy pathways reveal a noncanonical LC3 interacting region motif crucial for the enzymatic activity of human ATG3. ACS Central Science, 9(5), 1025-1034. https://doi.org/10.1021/acscentsci.3c00009 |
| Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology
Collu, G., Bierig, T., Krebs, A. S., Engilberge, S., Varma, N., Guixà-González, R., … Benoit, R. M. (2022). Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology. Structure, 30(1), 95-106. https://doi.org/10.1016/j.str.2021.09.002 |
| Design, expression, purification, and characterization of a YFP-tagged 2019-n CoV spike receptor-binding domain construct
Bierig, T., Collu, G., Blanc, A., Poghosyan, E., & Benoit, R. M. (2020). Design, expression, purification, and characterization of a YFP-tagged 2019-n CoV spike receptor-binding domain construct. Frontiers in Bioengineering and Biotechnology, 8, 618615 (10 pp.). https://doi.org/10.3389/fbioe.2020.618615 |
| Femtosecond-to-millisecond structural changes in a light-driven sodium pump
Skopintsev, P., Ehrenberg, D., Weinert, T., James, D., Kar, R. K., Johnson, P. J. M., … Standfuss, J. (2020). Femtosecond-to-millisecond structural changes in a light-driven sodium pump. Nature, 583, 314-318. https://doi.org/10.1038/s41586-020-2307-8 |
| Seamless insert-plasmid assembly at sub-terminal homologous sequences
Krebs, A. S., Bierig, T., Collu, G., & Benoit, R. M. (2019). Seamless insert-plasmid assembly at sub-terminal homologous sequences. Plasmid, 106, 102445 (9 pp.). https://doi.org/10.1016/j.plasmid.2019.102445 |
| Botulinum neurotoxin diversity from a gene-centered view
Benoit, R. M. (2018). Botulinum neurotoxin diversity from a gene-centered view. Toxins, 10(8), 310 (14 pp.). https://doi.org/10.3390/toxins10080310 |
| 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 |
| High-throughput mutagenesis using a two-fragment PCR approach
Heydenreich, F. M., Miljuš, T., Jaussi, R., Benoit, R., Milić, D., & Veprintsev, D. B. (2017). High-throughput mutagenesis using a two-fragment PCR approach. Scientific Reports, 7, 6787 (11 pp.). https://doi.org/10.1038/s41598-017-07010-4 |
| Seamless insert-plasmid assembly at high efficiency and low cost
Benoit, R. M., Ostermeier, C., Geiser, M., Li, J. S. Z., Widmer, H., & Auer, M. (2016). Seamless insert-plasmid assembly at high efficiency and low cost. PLoS One, 11(4), e0153158 (13 pp.). https://doi.org/10.1371/journal.pone.0153158 |
| 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 |
| Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten
Christen, P., Jaussi, R., & Benoit, R. (2016). Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten. https://doi.org/10.1007/978-3-662-46430-4 |
| 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 |
| Botulinum neurotoxins: new questions arising from structural biology
Kammerer, R. A., & Benoit, R. M. (2014). Botulinum neurotoxins: new questions arising from structural biology. Trends in Biochemical Sciences, 39(11), 517-526. https://doi.org/10.1016/j.tibs.2014.08.009 |
| The X-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible hur redox sensing mechanism
Benoit, R. M., Meisner, N. C., Kallen, J., Graff, P., Hemmig, R., Cèbe, R., … Auer, M. (2010). The X-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible hur redox sensing mechanism. Journal of Molecular Biology, 397(5), 1231-1244. https://doi.org/10.1016/j.jmb.2010.02.043 |
