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Structure–function dataset reveals environment effects within a fluorescent protein model system
De Zitter, E., Hugelier, S., Duwé, S., Vandenberg, W., Tebo, A. G., Van Meervelt, L., & Dedecker, P. (2021). Structure–function dataset reveals environment effects within a fluorescent protein model system. Angewandte Chemie International Edition, 60(18), 10073-10081. https://doi.org/10.1002/anie.202015201
Structural insights into the interaction of botulinum neurotoxin a with its neuronal receptor SV2C
Li, X., Brunner, C., Wu, Y., Leka, O., Schneider, G., & Kammerer, R. A. (2020). Structural insights into the interaction of botulinum neurotoxin a with its neuronal receptor SV2C. Toxicon, 175, 36-43. https://doi.org/10.1016/j.toxicon.2019.11.010
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
An overview of neutron scattering and molecular dynamics simulation studies of phospholipid bilayers in room-temperature ionic liquid/water solutions
Benedetto, A., & Ballone, P. (2018). An overview of neutron scattering and molecular dynamics simulation studies of phospholipid bilayers in room-temperature ionic liquid/water solutions. Physica B: Condensed Matter, 551, 227-231. https://doi.org/10.1016/j.physb.2018.02.043
Accelerating the association of the most stable protein–ligand complex by more than two orders of magnitude
Giese, C., Eras, J., Kern, A., Schärer, M. A., Capitani, G., & Glockshuber, R. (2016). Accelerating the association of the most stable protein–ligand complex by more than two orders of magnitude. Angewandte Chemie International Edition, 55(32), 9350-9355. https://doi.org/10.1002/anie.201603652
Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex
Pitchai, G. P., Hickson, I. D., Streicher, W., Montoya, G., & Mesa, P. (2016). Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 72, 646-651. https://doi.org/10.1107/S2053230X16010724
Direct inhibitors of InhA are active against Mycobacterium tuberculosis
Manjunatha, U. H., Rao, S. P. S., Kondreddi, R. R., Noble, C. G., Camacho, L. R., Tan, B. H., … Diagana, T. T. (2015). Direct inhibitors of InhA are active against Mycobacterium tuberculosis. Science Translational Medicine, 7(269). https://doi.org/10.1126/SCITRANSLMED.3010597
Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB
Eicher, T., Seeger, M. A., Anselmi, C., Zhou, W., Brandstätter, L., Verrey, F., … Pos, K. M. (2014). Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB. eLife, 3. https://doi.org/10.7554/eLife.03145
Structure and substrate ion binding in the sodium/proton antiporter PaNhaP
Wöhlert, D., Kühlbrandt, W., & Yildiz, O. (2014). Structure and substrate ion binding in the sodium/proton antiporter PaNhaP. eLife, 3, e03579. https://doi.org/10.7554/eLife.03579
The thermodynamic influence of trapped water molecules on a protein-ligand interaction
Stegmann, C. M., Seeliger, D., Sheldrick, G. M., de Groot, B. L., & Wahl, M. C. (2009). The thermodynamic influence of trapped water molecules on a protein-ligand interaction. Angewandte Chemie International Edition, 48(28), 5207-5210. https://doi.org/10.1002/anie.200900481