| Bridging the maytansine and vinca sites: Cryptophycins target β-tubulin's T5-loop
Abel, A. C., Mühlethaler, T., Dessin, C., Schachtsiek, T., Sammet, B., Sharpe, T., … Prota, A. E. (2024). Bridging the maytansine and vinca sites: Cryptophycins target β-tubulin's T5-loop. Journal of Biological Chemistry, 300(6), 107363 (10 pp.). https://doi.org/10.1016/j.jbc.2024.107363 |
| Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography
Cellini, A., Shankar, M. K., Nimmrich, A., Hunt, L. A., Monrroy, L., Mutisya, J., … Westenhoff, S. (2024). Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography. Nature Chemistry, 16, 624-632. https://doi.org/10.1038/s41557-023-01413-9 |
| 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 |
| Structural basis of connexin-36 gap junction channel inhibition
Ding, X., Aureli, S., Vaithia, A., Lavriha, P., Schuster, D., Khanppnavar, B., … Korkhov, V. M. (2024). Structural basis of connexin-36 gap junction channel inhibition. Cell Discovery, 10(1), 68 (4 pp.). https://doi.org/10.1038/s41421-024-00691-y |
| Capturing the blue-light activated state of the Phot-LOV1 domain from <em>Chlamydomonas reinhardtii </em>using time-resolved serial synchrotron crystallography
Gotthard, G., Mous, S., Weinert, T., Maia, R. N. A., James, D., Dworkowski, F., … Nogly, P. (2024). Capturing the blue-light activated state of the Phot-LOV1 domain from Chlamydomonas reinhardtii using time-resolved serial synchrotron crystallography. IUCrJ, 11(5) (17 pp.). https://doi.org/10.1107/S2052252524005608 |
| Fixed-target pump–probe SFX: eliminating the scourge of light contamination
Gotthard, G., Flores-Ibarra, A., Carrillo, M., Kepa, M. W., Mason, T. J., Stegmann, D. P., … Nogly, P. (2024). Fixed-target pump–probe SFX: eliminating the scourge of light contamination. IUCrJ, 11(5), 1-13. https://doi.org/10.1107/S2052252524005591 |
| Systematic identification of structure-specific protein–protein interactions
Holfeld, A., Schuster, D., Sesterhenn, F., Gillingham, A. K., Stalder, P., Haenseler, W., … Picotti, P. (2024). Systematic identification of structure-specific protein–protein interactions. Molecular Systems Biology, 20, 651-675. https://doi.org/10.1038/s44320-024-00037-6 |
| Modular synthesis of functional libraries by accelerated SuFEx click chemistry
Homer, J. A., Koelln, R. A., Barrow, A. S., Gialelis, T. L., Boiarska, Z., Steinohrt, N. S., … Moses, J. E. (2024). Modular synthesis of functional libraries by accelerated SuFEx click chemistry. Chemical Science, 15, 3879-3892. https://doi.org/10.1039/d3sc05729a |
| Comprehensive overview of bottom-up proteomics using mass spectrometry
Jiang, Y., Rex, D. A. B., Schuster, D., Neely, B. A., Rosano, G. L., Volkmar, N., … Meyer, J. G. (2024). Comprehensive overview of bottom-up proteomics using mass spectrometry. ACS Measurement Science Au, 4(4), 338-417. https://doi.org/10.1021/acsmeasuresciau.3c00068 |
| Advances, challenges, and opportunities in structural biology
Khanppnavar, B., North, R. A., Ventura, S., & Xu, Y. (2024). Advances, challenges, and opportunities in structural biology. Trends in Biochemical Sciences, 49(2), 93-96. https://doi.org/10.1016/j.tibs.2023.12.006 |
| Regulatory sites of CaM-sensitive adenylyl cyclase AC8 revealed by cryo-EM and structural proteomics
Khanppnavar, B., Schuster, D., Lavriha, P., Uliana, F., Özel, M., Mehta, V., … Korkhov, V. M. (2024). Regulatory sites of CaM-sensitive adenylyl cyclase AC8 revealed by cryo-EM and structural proteomics. EMBO Reports, 25, 1513-1540. https://doi.org/10.1038/s44319-024-00076-y |
| Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase
Khanppnavar, B., Choo, J. P. S., Hagedoorn, P. L., Smolentsev, G., Štefanić, S., Kumaran, S., … Li, X. (2024). Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase. Nature Chemistry, 16, 1496-1504. https://doi.org/10.1038/s41557-024-01523-y |
| The time revolution in macromolecular crystallography
Khusainov, G., Standfuss, J., & Weinert, T. (2024). The time revolution in macromolecular crystallography. Structural Dynamics, 11(2), 020901 (17 pp.). https://doi.org/10.1063/4.0000247 |
| Expression, purification, and nanodisc reconstitution of connexin-43 hemichannels for structural characterization by cryo-electron microscopyp
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| Microtubule specialization by +TIP networks: from mechanisms to functional implications
Meier, S. M., Steinmetz, M. O., & Barral, Y. (2024). Microtubule specialization by +TIP networks: from mechanisms to functional implications. Trends in Biochemical Sciences, 49(4), 318-332. https://doi.org/10.1016/j.tibs.2024.01.005 |
| Three-dimensional microfluidic capillary device for rapid and multiplexed immunoassays in whole blood
Mortelmans, T., Marty, B., Kazazis, D., Padeste, C., Li, X., & Ekinci, Y. (2024). Three-dimensional microfluidic capillary device for rapid and multiplexed immunoassays in whole blood. ACS Sensors, 9(5), 2455-2464. https://doi.org/10.1021/acssensors.4c00153 |
| A photo-SAR study of photoswitchable azobenzene tubulin-inhibiting antimitotics identifying a general method for near-quantitative photocontrol
Reynders, M., Garścia, M., Müller-Deku, A., Wranik, M., Krauskopf, K., de la Osa de la Rosa, L., … Thorn-Seshold, O. (2024). A photo-SAR study of photoswitchable azobenzene tubulin-inhibiting antimitotics identifying a general method for near-quantitative photocontrol. Chemical Science, 15(31), 12301-12309. https://doi.org/10.1039/d4sc03072a |
| Activating an invertebrate bistable opsin with the all-trans 6.11 retinal analog
Rodrigues, M. J., Tejero, O., Mühle, J., Pamula, F., Das, I., Tsai, C. J., … Schertler, G. F. X. (2024). Activating an invertebrate bistable opsin with the all-trans 6.11 retinal analog. Proceedings of the National Academy of Sciences of the United States of America PNAS, 121(31), e2406814121 (3 pp.). https://doi.org/10.1073/pnas.2406814121 |
| Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor
Saha, S., Khanppnavar, B., Maharana, J., Kim, H., Carino, C. M. C., Daly, C., … Shukla, A. K. (2024). Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor. Cell, 187(17), 4751-4769.e25. https://doi.org/10.1016/j.cell.2024.07.005 |
| Structural insights into membrane adenylyl cyclases, initiators of cAMP signaling
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