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Nanomagnetic encoding of shape-morphing micromachines
Cui, J., Huang, T. Y., Luo, Z., Testa, P., Gu, H., Chen, X. Z., … Heyderman, L. J. (2019). Nanomagnetic encoding of shape-morphing micromachines. Nature, 575(7781), 164-168. https://doi.org/10.1038/s41586-019-1713-2
The ultrafast Einstein–de Haas effect
Dornes, C., Acremann, Y., Savoini, M., Kubli, M., Neugebauer, M. J., Abreu, E., … Johnson, S. L. (2019). The ultrafast Einstein–de Haas effect. Nature, 565(7738), 209-212. https://doi.org/10.1038/s41586-018-0822-7
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
Verschueren, K. H. G., Blanchet, C., Felix, J., Dansercoer, A., De Vos, D., Bloch, Y., … Verstraete, K. (2019). Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature, 568(7753), 571-575. https://doi.org/10.1038/s41586-019-1095-5
Triggers of tree mortality under drought
Choat, B., Brodribb, T. J., Brodersen, C. R., Duursma, R. A., López, R., & Medlyn, B. E. (2018). Triggers of tree mortality under drought. Nature, 558(7711), 531-539. https://doi.org/10.1038/s41586-018-0240-x
Structure of a volume-regulated anion channel of the LRRC8 family
Deneka, D., Sawicka, M., Lam, A. K. M., Paulino, C., & Dutzler, R. (2018). Structure of a volume-regulated anion channel of the LRRC8 family. Nature, 558(7709), 254-259. https://doi.org/10.1038/s41586-018-0134-y
Methicillin-resistant Staphylococcus aureus alters cell wall glycosylation to evade immunity
Gerlach, D., Guo, Y., De Castro, C., Kim, S. H., Schlatterer, K., Xu, F. F., … Peschel, A. (2018). Methicillin-resistant Staphylococcus aureus alters cell wall glycosylation to evade immunity. Nature, 563(7733), 705-709. https://doi.org/10.1038/s41586-018-0730-x
Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination
Kalayil, S., Bhogaraju, S., Bonn, F., Shin, D., Liu, Y., Gan, N., … Dikic, I. (2018). Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination. Nature, 557(7707), 734-738. https://doi.org/10.1038/s41586-018-0145-8
Structure of the μ–opioid receptor–G<sub>i</sub> protein complex
Koehl, A., Hu, H., Maeda, S., Zhang, Y., Qu, Q., Paggi, J. M., … Kobilka, B. K. (2018). Structure of the μ–opioid receptor–Gi protein complex. Nature, 558(7711), 547-552. https://doi.org/10.1038/s41586-018-0219-7
Tc toxin activation requires unfolding and refolding of a beta-propeller
Kuhlee, A. (2018). Tc toxin activation requires unfolding and refolding of a beta-propeller. Nature, 563(7730), 209. https://doi.org/10.1038/s41586-018-0556-6
Magnetoelectric inversion of domain patterns
Leo, N., Carolus, V., White, J. S., Kenzelmann, M., Hudl, M., Tolédano, P., … Fiebig, M. (2018). Magnetoelectric inversion of domain patterns. Nature, 560(7719), 466-470. https://doi.org/10.1038/s41586-018-0432-4
Soft-tissue evidence for homeothermy and crypsis in a Jurassic ichthyosaur
Lindgren, J., Sjövall, P., Thiel, V., Zheng, W., Ito, S., Wakamatsu, K., … Schweitzer, M. H. (2018). Soft-tissue evidence for homeothermy and crypsis in a Jurassic ichthyosaur. Nature, 564(7736), 359-365. https://doi.org/10.1038/s41586-018-0775-x
Probing the interatomic potential of solids with strong-field nonlinear phononics
Von Hoegen, A., Mankowsky, R., Fechner, M., Först, M., & Cavalleri, A. (2018). Probing the interatomic potential of solids with strong-field nonlinear phononics. Nature, 555(7694), 79-82. https://doi.org/10.1038/nature25484
Structure of activated transcription complex Pol II–DSIF–PAF–SPT6
Vos, S. M., Farnung, L., Boehning, M., Wigge, C., Linden, A., Urlaub, H., & Cramer, P. (2018). Structure of activated transcription complex Pol II–DSIF–PAF–SPT6. Nature, 560(7720), 607-612. https://doi.org/10.1038/s41586-018-0440-4
CGAS senses long and HMGB/TFAM-bound U-turn DNA by forming protein-DNA ladders
Andreeva, L., Hiller, B., Kostrewa, D., Lässig, C., De Oliveira Mann, C. C., Jan Drexler, D., … Hopfner, K. P. (2017). CGAS senses long and HMGB/TFAM-bound U-turn DNA by forming protein-DNA ladders. Nature, 549(7672), 394-398. https://doi.org/10.1038/nature23890
Three-dimensional magnetization structures revealed with X-ray vector nanotomography
Donnelly, C., Guizar-Sicairos, M., Scagnoli, V., Gliga, S., Holler, M., Raabe, J., & Heyderman, L. J. (2017). Three-dimensional magnetization structures revealed with X-ray vector nanotomography. Nature, 547(7663), 328-331. https://doi.org/10.1038/nature23006
High-resolution non-destructive three-dimensional imaging of integrated circuits
Holler, M., Guizar-Sicairos, M., Tsai, E. H. R., Dinapoli, R., Müller, E., Bunk, O., … Aeppli, G. (2017). High-resolution non-destructive three-dimensional imaging of integrated circuits. Nature, 543(7645), 402-406. https://doi.org/10.1038/nature21698
Crystal structures of agonist-bound human cannabinoid receptor CB 1
Hua, T., Vemuri, K., Nikas, S. P., Laprairie, R. B., Wu, Y., Qu, L., … Liu, Z. J. (2017). Crystal structures of agonist-bound human cannabinoid receptor CB 1. Nature, 547(7664), 468-471. https://doi.org/10.1038/nature23272
Catalyst support effects on hydrogen spillover
Karim, W., Spreafico, C., Kleibert, A., Gobrecht, J., VandeVondele, J., Ekinci, Y., & van Bokhoven, J. A. (2017). Catalyst support effects on hydrogen spillover. Nature, 541(7635), 68-71. https://doi.org/10.1038/nature20782
Observation of three-component fermions in the topological semimetal molybdenum phosphide
Lv, B. Q., Feng, Z. L., Xu, Q. N., Gao, X., Ma, J. Z., Kong, L. Y., … Ding, H. (2017). Observation of three-component fermions in the topological semimetal molybdenum phosphide. Nature, 546(7660), 627-631. https://doi.org/10.1038/nature22390
Core Mediator structure at 3.4 Å extends model of transcription initiation complex
Nozawa, K., Schneider, T. R., & Cramer, P. (2017). Core Mediator structure at 3.4 Å extends model of transcription initiation complex. Nature, 545(7653), 248-251. https://doi.org/10.1038/nature22328
 

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