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Efficient production of a functional G protein-coupled receptor in <em>E. coli</em> for structural studies
Abiko, L. A., Rogowski, M., Gautier, A., Schertler, G., & Grzesiek, S. (2021). Efficient production of a functional G protein-coupled receptor in E. coli for structural studies. Journal of Biomolecular NMR, 75(1), 25-38. https://doi.org/10.1007/s10858-020-00354-6
A set of common movements within GPCR-G-protein complexes from variability analysis of cryo-EM datasets
Marino, J., & Schertler, G. F. X. (2021). A set of common movements within GPCR-G-protein complexes from variability analysis of cryo-EM datasets. Journal of Structural Biology, 213(2), 107699 (7 pp.). https://doi.org/10.1016/j.jsb.2021.107699
Biochemical characterization of GPCR-G protein complex formation
Pamula, F., & Tsai, C. J. (2021). Biochemical characterization of GPCR-G protein complex formation. In I. Schmidt-Krey & J. C. Gumbart (Eds.), Methods in molecular biology: Vol. 2302. Structure and function of membrane proteins (pp. 37-48). https://doi.org/10.1007/978-1-0716-1394-8_3
Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron
Aumonier, S., Santoni, G., Gotthard, G., von Stetten, D., Leonard, G. A., & Royant, A. (2020). Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron. IUCrJ, 7, 728-736. https://doi.org/10.1107/S2052252520007411
Immobilization of arrestin-3 on different biosensor platforms for evaluating GPCR binding
Avsar, S. Y., Kapinos, L. E., Schoenenberger, C. A., Schertler, G. F. X., Mühle, J., Meger, B., … Palivan, C. G. (2020). Immobilization of arrestin-3 on different biosensor platforms for evaluating GPCR binding. Physical Chemistry Chemical Physics, 22(41), 24086-24096. https://doi.org/10.1039/d0cp01464h
Soluble dimeric prion protein ligand activates Adgrg6 receptor but does not rescue early signs of demyelination in PrP-deficient mice
Henzi, A., Senatore, A., Lakkaraju, A. K. K., Scheckel, C., Mühle, J., Reimann, R., … Aguzzi, A. (2020). Soluble dimeric prion protein ligand activates Adgrg6 receptor but does not rescue early signs of demyelination in PrP-deficient mice. PLoS One, 15(11), e0242137 (22 pp.). https://doi.org/10.1371/journal.pone.0242137
Light-sensitive membrane proteins as tools to generate precision treatments
Lesca, E. (2020). Light-sensitive membrane proteins as tools to generate precision treatments. Journal of Membrane Biology, 253(2), 81-86. https://doi.org/10.1007/s00232-020-00115-4
The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in <em>Enterococcus faecalis</em> quorum sensing
Littlewood, S., Tattersall, H., Hughes, C. S., Hussain, R., Ma, P., Harding, S. E., … Phillips-Jones, M. K. (2020). The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in Enterococcus faecalis quorum sensing. FEBS Letters, 594(3), 553-563. https://doi.org/10.1002/1873-3468.13634
Crystal structure of mannose specific IIA subunit of phosphotransferase system from <em>Streptococcus pneumoniae</em>
Magoch, M., Nogly, P., Grudnik, P., Ma, P., Boczkus, B., Neves, A. R., … Dubin, G. (2020). Crystal structure of mannose specific IIA subunit of phosphotransferase system from Streptococcus pneumoniae. Molecules, 25(20), 4633 (13 pp.). https://doi.org/10.3390/molecules25204633
GPCR solubilization and quality control
Miljus, T., Sykes, D. A., Harwood, C. R., Vuckovic, Z., & Veprintsev, D. B. (2020). GPCR solubilization and quality control. In C. Perez & T. Maier (Eds.), Methods in molecular biology: Vol. 2127. Expression, purification, and structural biology of membrane proteins (pp. 105-127). https://doi.org/10.1007/978-1-0716-0373-4_8
Advances in long-wavelength native phasing at X-ray free-electron lasers
Nass, K., Cheng, R., Vera, L., Mozzanica, A., Redford, S., Ozerov, D., … Milne, C. J. (2020). Advances in long-wavelength native phasing at X-ray free-electron lasers. IUCrJ, 7, 965-975. https://doi.org/10.1107/S2052252520011379
Strategic screening and characterization of the visual GPCR-mini-G protein signaling complex for successful crystallization
Pamula, F., Mühle, J., Blanc, A., Nehmé, R., Edwards, P. C., Tate, C. G., & Tsai, C. J. (2020). Strategic screening and characterization of the visual GPCR-mini-G protein signaling complex for successful crystallization. Journal of Visualized Experiments (157), e60747 (10 pp.). https://doi.org/10.3791/60747
GPCR activation states induced by nanobodies and mini-G proteins compared by NMR spectroscopy
Rößler, P., Mayer, D., Tsai, C. J., Veprintsev, D. B., Schertler, G. F. X., & Gossert, A. D. (2020). GPCR activation states induced by nanobodies and mini-G proteins compared by NMR spectroscopy. Molecules, 25(24), 5984 (17 pp.). https://doi.org/10.3390/molecules25245984
Conservation of gene architecture and domains amidst sequence divergence in the &lt;em&gt;hsrω &lt;/em&gt;lncRNA gene across the &lt;em&gt;Drosophila &lt;/em&gt;genus: an &lt;em&gt;in silico&lt;/em&gt; analysis
Sahu, R. K., Mutt, E., & Lakhotia, S. C. (2020). Conservation of gene architecture and domains amidst sequence divergence in the hsrω lncRNA gene across the Drosophila genus: an in silico analysis. Journal of Genetics, 99(1), 64 (26 pp.). https://doi.org/10.1007/s12041-020-01218-6
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
Membrane protein preparation for serial crystallography using high-viscosity injectors: rhodopsin as an example
Weinert, T., & Panneels, V. (2020). Membrane protein preparation for serial crystallography using high-viscosity injectors: rhodopsin as an example. In C. Perez & T. Maier (Eds.), Methods in molecular biology: Vol. 2127. Expression, purification, and structural biology of membrane proteins (pp. 321-338). https://doi.org/10.1007/978-1-0716-0373-4_21
Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals
Casadei, C. M., Nass, K., Barty, A., Hunter, M. S., Padeste, C., Tsai, C. J., … Pedrini, B. (2019). Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals. IUCrJ, 6, 34-45. https://doi.org/10.1107/S2052252518014641
The two-photon reversible reaction of the bistable jumping spider rhodopsin-1
Ehrenberg, D., Varma, N., Deupi, X., Koyanagi, M., Terakita, A., Schertler, G. F. X., … Lesca, E. (2019). The two-photon reversible reaction of the bistable jumping spider rhodopsin-1. Biophysical Journal, 116(7), 1248-1258. https://doi.org/10.1016/j.bpj.2019.02.025
Insights into the basal activity and activation mechanism of the β1 adrenergic receptor using native mass spectrometry
Gavriilidou, A. F. M., Hunziker, H., Mayer, D., Vuckovic, Z., Veprintsev, D. B., & Zenobi, R. (2019). Insights into the basal activity and activation mechanism of the β1 adrenergic receptor using native mass spectrometry. Journal of the American Society for Mass Spectrometry, 30(3), 529-537. https://doi.org/10.1007/s13361-018-2110-z
Arrestin-1 engineering facilitates complex stabilization with native rhodopsin
Haider, R. S., Wilhelm, F., Rizk, A., Mutt, E., Deupi, X., Peterhans, C., … Ostermaier, M. K. (2019). Arrestin-1 engineering facilitates complex stabilization with native rhodopsin. Scientific Reports, 9(1), 439 (13 pp.). https://doi.org/10.1038/s41598-018-36881-4
 

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