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Spin cascade and doming in ferric hemes: femtosecond X-ray absorption and X-ray emission studies
Bacellar, C., Kinschel, D., Mancini, G. F., Ingle, R. A., Rouxel, J., Cannelli, O., … Chergui, M. (2020). Spin cascade and doming in ferric hemes: femtosecond X-ray absorption and X-ray emission studies. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(36), 21914-21920. https://doi.org/10.1073/pnas.2009490117
Electron-phonon-driven three-dimensional metallicity in an insulating cuprate
Baldini, E., Sentef, M. A., Acharya, S., Brumme, T., Sheveleva, E., Lyzwa, F., … Weber, C. (2020). Electron-phonon-driven three-dimensional metallicity in an insulating cuprate. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(12), 6409-6416. https://doi.org/10.1073/pnas.1919451117
Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation
Dubey, B. N., Agustoni, E., Böhm, R., Kaczmarczyk, A., Mangia, F., von Arx, C., … Schirmer, T. (2020). Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(2), 1000-1008. https://doi.org/10.1073/pnas.1911427117
Natural hybrid silica/protein superstructure at atomic resolution
Görlich, S., Samuel, A. J., Best, R. J., Seidel, R., Vacelet, J., Leonarski, F. K., … Zlotnikov, I. (2020). Natural hybrid silica/protein superstructure at atomic resolution. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(49), 31088-31093. https://doi.org/10.1073/pnas.2019140117
A precisely positioned MED12 activation helix stimulates CDK8 kinase activity
Klatt, F., Leitner, A., Kim, I. V., Ho-Xuan, H., Schneider, E. V., Langhammer, F., … Kuhn, C. D. (2020). A precisely positioned MED12 activation helix stimulates CDK8 kinase activity. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(6), 2894-2905. https://doi.org/10.1073/pnas.1917635117
A lipocalin mediates unidirectional heme biomineralization in malaria parasites
Matz, J. M., Drepper, B., Blum, T. B., van Genderen, E., Burrell, A., Martin, P., … Blackman, M. J. (2020). A lipocalin mediates unidirectional heme biomineralization in malaria parasites. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(28), 16546-16556. https://doi.org/10.1073/pnas.2001153117
Structural basis for recognition of RALF peptides by LRX proteins during pollen tube growth
Moussu, S., Broyart, C., Santos-Fernandez, G., Augustin, S., Wehrle, S., Grossniklaus, U., & Santiago, J. (2020). Structural basis for recognition of RALF peptides by LRX proteins during pollen tube growth. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(13), 7494-7503. https://doi.org/10.1073/pnas.2000100117
Impact shock origin of diamonds in ureilite meteorites
Nestola, F., Goodrich, C. A., Morana, M., Barbaro, A., Jakubek, R. S., Christ, O., … Shaddad, M. H. (2020). Impact shock origin of diamonds in ureilite meteorites. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(41), 25310-25318. https://doi.org/10.1073/pnas.1919067117
Molecular mechanism for the recognition of sequencedivergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2
Okuda, S., Fujita, S., Moretti, A., Hohmann, U., Doblas, V. G., Ma, Y., … Hothorn, M. (2020). Molecular mechanism for the recognition of sequencedivergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(5), 2693-2703. https://doi.org/10.1073/pnas.1911553117
Strain engineering of the charge and spin-orbital interactions in Sr<sub>2</sub>IrO<sub>4</sub>
Paris, E., Tseng, Y., Pärschke, E. M., Zhang, W., Upton, M. H., Efimenko, A., … Schmitt, T. (2020). Strain engineering of the charge and spin-orbital interactions in Sr2IrO4. Proceedings of the National Academy of Sciences of the United States of America PNAS. https://doi.org/10.1073/pnas.2012043117
Load-induced dynamical transitions at graphene interfaces
Peng, D., Wu, Z., Shi, D., Qu, C., Jiang, H., Song, Y., … Zheng, Q. (2020). Load-induced dynamical transitions at graphene interfaces. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(23), 12618-12623. https://doi.org/10.1073/pnas.1922681117
Fibroblast rejuvenation by mechanical reprogramming and redifferentiation
Roy, B., Yuan, L., Lee, Y., Bharti, A., Mitra, A., & Shivashankar, G. V. (2020). Fibroblast rejuvenation by mechanical reprogramming and redifferentiation. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(19), 10131-10141. https://doi.org/10.1073/pnas.1911497117
Multiphase magnetism in Yb<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>
Scheie, A., Kindervater, J., Zhang, S., Changlani, H. J., Sala, G., Ehlers, G., … Broholm, C. (2020). Multiphase magnetism in Yb2Ti2O7. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(44), 27245-27254. https://doi.org/10.1073/pnas.2008791117
Structural basis for DEAH-helicase activation by G-patch proteins
Studer, M. K., Ivanovic, L., Weber, M. E., Marti, S., & Jonas, S. (2020). Structural basis for DEAH-helicase activation by G-patch proteins. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(13), 7159-7170. https://doi.org/10.1073/pnas.1913880117
Quantum spin-liquid states in an organic magnetic layer and molecular rotor hybrid
Szirmai, P., Mézière, C., Bastien, G., Wzietek, P., Batail, P., Martino, E., … Náfrádi, B. (2020). Quantum spin-liquid states in an organic magnetic layer and molecular rotor hybrid. Proceedings of the National Academy of Sciences of the United States of America PNAS, 117(47), 29555-29560. https://doi.org/10.1073/pnas.2000188117
Unraveling intrinsic correlation effects with angle-resolved photoemission spectroscopy
Zhou, J. S., Reining, L., Nicolaou, A., Bendounan, A., Ruotsalainen, K., Vanzini, M., … Gatti, M. (2020). Unraveling intrinsic correlation effects with angle-resolved photoemission spectroscopy. Proceedings of the National Academy of Sciences of the United States of America PNAS. https://doi.org/10.1073/pnas.2012625117
Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism
Brünle, S., Eisinger, M. L., Poppe, J., Mills, D. J., Langer, J. D., Vonck, J., & Ermler, U. (2019). Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism. Proceedings of the National Academy of Sciences of the United States of America PNAS, 116(52), 26497-26504. https://doi.org/10.1073/pnas.1913031116
Crystal structure of <em>cis</em>-aconitate decarboxylase reveals the impact of naturally occurring human mutations on itaconate synthesis
Chen, F., Lukat, P., Iqbal, A. A., Saile, K., Kaever, V., van den Heuvel, J., … Pessler, F. (2019). Crystal structure of cis-aconitate decarboxylase reveals the impact of naturally occurring human mutations on itaconate synthesis. Proceedings of the National Academy of Sciences of the United States of America PNAS, 116(41), 20644-20654. https://doi.org/10.1073/pnas.1908770116
Organism motility in an oxygenated shallow-marine environment 2.1 billion years ago
El Albani, A., Gabriela Mangano, M., Buatois, L. A., Bengtson, S., Riboulleau, A., Bekker, A., … Canfield, D. E. (2019). Organism motility in an oxygenated shallow-marine environment 2.1 billion years ago. Proceedings of the National Academy of Sciences of the United States of America PNAS, 116(9), 3431-3436. https://doi.org/10.1073/pnas.1815721116
Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites
Hemmann, J. L., Wagner, T., Shima, S., & Vorholt, J. A. (2019). Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites. Proceedings of the National Academy of Sciences of the United States of America PNAS, 116(51), 25583-25590. https://doi.org/10.1073/pnas.1911595116
 

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