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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. https://doi.org/10.1007/978-1-0716-0373-4_21
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
Structural basis for allosteric ligand recognition in the human CC chemokine receptor 7
Jaeger, K., Bruenle, S., Weinert, T., Guba, W., Muehle, J., Miyazaki, T., … Standfuss, J. (2019). Structural basis for allosteric ligand recognition in the human CC chemokine receptor 7. Cell, 178(5), 1222-1230. https://doi.org/10.1016/j.cell.2019.07.028
Improving high viscosity extrusion of microcrystals for time-resolved serial femtosecond crystallography at X-ray lasers
James, D., Weinert, T., Skopintsev, P., Furrer, A., Gashi, D., Tanaka, T., … Standfuss, J. (2019). Improving high viscosity extrusion of microcrystals for time-resolved serial femtosecond crystallography at X-ray lasers. Journal of Visualized Experiments, (144), e59087. https://doi.org/10.3791/59087
Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Mayer, D., Damberger, F. F., Samarasimhareddy, M., Feldmueller, M., Vuckovic, Z., Flock, T., … Veprintsev, D. B. (2019). Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation. Nature Communications, 10, 1261 (14 pp.). https://doi.org/10.1038/s41467-019-09204-y
Alkyladenine DNA glycosylase associates with transcription elongation to coordinate DNA repair with gene expression
Montaldo, N. P., Bordin, D. L., Brambilla, A., Rösinger, M., Fordyce Martin, S. L., Bjørås, K. Ø., … van Loon, B. (2019). Alkyladenine DNA glycosylase associates with transcription elongation to coordinate DNA repair with gene expression. Nature Communications, 10(1), 5460 (13 pp.). https://doi.org/10.1038/s41467-019-13394-w
Membrane protein dynamics studied by X-ray lasers - or why only time will tell
Standfuss, J. (2019). Membrane protein dynamics studied by X-ray lasers - or why only time will tell. Current Opinion in Structural Biology, 57, 63-71. https://doi.org/10.1016/j.sbi.2019.02.001
Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography
Weinert, T., Skopintsev, P., James, D., Dworkowski, F., Panepucci, E., Kekilli, D., … Standfuss, J. (2019). Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science, 365(6448), 61-65. https://doi.org/10.1126/science.aaw8634
Bacteriorhodopsin: structural insights revealed using X-ray lasers and synchrotron radiation
Wickstrand, C., Nogly, P., Nango, E., Iwata, S., Standfuss, J., & Neutze, R. (2019). Bacteriorhodopsin: structural insights revealed using X-ray lasers and synchrotron radiation. Annual Review of Biochemistry, 88, 59-83. https://doi.org/10.1146/annurev-biochem-013118-111327
CLASP suppresses microtubule catastrophes through a single TOG domain
Aher, A., Kok, M., Sharma, A., Rai, A., Olieric, N., Rodriguez-Garcia, R., … Akhmanova, A. (2018). CLASP suppresses microtubule catastrophes through a single TOG domain. Developmental Cell, 46(1), 40-58.e8. https://doi.org/10.1016/j.devcel.2018.05.032
Seeded X-ray free-electron laser generating radiation with laser statistical properties
Gorobtsov, O. Y., Mercurio, G., Capotondi, F., Skopintsev, P., Lazarev, S., Zaluzhnyy, I. A., … Vartanyants, I. A. (2018). Seeded X-ray free-electron laser generating radiation with laser statistical properties. Nature Communications, 9(1), 4498 (6 pp.). https://doi.org/10.1038/s41467-018-06743-8
In situ serial crystallography for rapid de novo membrane protein structure determination.
Huang, C. Y., Olieric, V., Howe, N., Warshamanage, R., Weinert, T., Panepucci, E., … Wang, M. (2018). In situ serial crystallography for rapid de novo membrane protein structure determination. Communications Biology, 1, 124 (8 pp.). https://doi.org/10.1038/S42003-018-0123-6
Ligand channel in pharmacologically stabilized rhodopsin
Mattle, D., Kuhn, B., Aebi, J., Bedoucha, M., Kekilli, D., Grozinger, N., … Dawson, R. J. P. (2018). Ligand channel in pharmacologically stabilized rhodopsin. Proceedings of the National Academy of Sciences of the United States of America PNAS, 115(14), 3640-3645. https://doi.org/10.1073/pnas.1718084115
Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser
Nogly, P., Weinert, T., James, D., Carbajo, S., Ozerov, D., Furrer, A., … Standfuss, J. (2018). Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science, 361(6398), eaat0094 (7 pp.). https://doi.org/10.1126/science.aat0094
Quantitative ptychographic bio-imaging in the water window
Rose, M., Senkbeil, T., von Gundlach, A. R., Stuhr, S., Rumancev, C., Dzhigaev, D., … Vartanyants, I. A. (2018). Quantitative ptychographic bio-imaging in the water window. Optics Express, 26(2), 1237-1254. https://doi.org/10.1364/OE.26.001237
Crystal structure of rhodopsin in complex with a mini-G<sub>o</sub> sheds light on the principles of G protein selectivity
Tsai, C. J., Pamula, F., Nehmé, R., Mühle, J., Weinert, T., Flock, T., … Schertler, G. F. X. (2018). Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of G protein selectivity. Science Advances, 4(9), aat7052 (9 pp.). https://doi.org/10.1126/sciadv.aat7052