Parties d'ouvrages collectifs (2)
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Huculeci, R. I., Kieken, F., Garcia-Pino, A., Buts, L., van Nuland, N. A. J., & Lenaerts, T. (2017). Structural characterization of monomeric/dimeric state of p59fyn SH2 domain. In K. Machida & B. Liu (Eds.), SH2 Domains: Methods and Protocols (1 ed., p. 555). Humana Press. Articles dans des revues avec comité de lecture (76)
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Ainelo, A., Caballero-Montes, J., Bulvas, O., Ernits, K., Coppieters'T Wallant, K., Takada, H., Craig, S., Mazzucchelli, G., Zedek, S., Pichová, I. I., Atkinson, G. C., Talavera Perez, A., Martens, C., Hauryliuk, V., & Garcia-Pino, A. (2023). The structure of DarB in complex with Rel NTD reveals nonribosomal activation of Rel stringent factors. Science advances, 9(3). doi:10.1126/sciadv.ade40772.
Tamman, H., Ernits, K., Roghanian, M., Ainelo, A., Julius, C., Perrier, A., Talavera Perez, A., Ainelo, H., Dugauquier, R., Zedek, S., Thureau, A., Pérez, J., Mendez, G. L., Hallez, R., Atkinson, G. C., Hauryliuk, V., & Garcia-Pino, A. (2022). Structure of SpoT reveals evolutionary tuning of catalysis via conformational constraint. Nature Chemical Biology. doi:10.1038/s41589-022-01198-x3.
Zhang, T., Tamman, H., Coppieters'T Wallant, K., Kurata, T., LeRoux, M., Srikant, S., Brodiazhenko, T., Cepauskas, A., Talavera Perez, A., Martens, C., Atkinson, G. C., Hauryliuk, V., Garcia-Pino, A., & Laub, M. T. (2022). Direct activation of a bacterial innate immune system by a viral capsid protein. Nature (London), 612(7938), 132-140. doi:10.1038/s41586-022-05444-z4.
Mojr, V., Roghanian, M., Tamman, H., Do Pham, D. D., Petrová, M., Pohl, R., Takada, H., Van Nerom, K., Ainelo, H., Caballero Montes, J., Jimmy, S., Garcia-Pino, A., Hauryliuk, V., & Rejman, D. (2021). Nonhydrolysable Analogues of (p)ppGpp and (p)ppApp Alarmone Nucleotides as Novel Molecular Tools. A C S Chemical Biology. doi:10.1021/acschembio.1c003985.
Scholl, D., Sigoillot, M., Overtus, M., Colomer Martinez, R., Martens, C., Wang, Y. Y., Pardon, E., Laeremans, T., Garcia-Pino, A., Steyaert, J., Sheppard, D. N., Hendrix, J., & Govaerts, C. (2021). A Topological Switch in the Cystic Fibrosis Transmembrane Conductance Regulator Modulates Channel Activity and Sensitivity to Disease-Causing Mutation. Nature Chemical Biology. doi:10.1038/s41589-021-00844-06.
Kurata, T., Brodiazhenko, T., Alves Oliveira, S. R., Roghanian, M., Sakaguchi, Y., Turnbull, K. J., Bulvas, O., Takada, H., Tamman, H., Ainelo, A., Pohl, R., Rejman, D., Tenson, T., Suzuki, T., Garcia-Pino, A., Atkinson, G. C., & Hauryliuk, V. (2021). RelA-SpoT Homolog toxins pyrophosphorylate the CCA end of tRNA to inhibit protein synthesis. Molecular cell, 81(15), 3160-3170.e9. doi:10.1016/j.molcel.2021.06.0057.
Roghanian, M., Van Nerom, K., Takada, H., Caballero Montes, J., Tamman, H., Kudrin, P., Talavera Perez, A., Dzhygyr, I., Ekström, S., Atkinson, G. C., Garcia-Pino, A., & Hauryliuk, V. (2021). (p)ppGpp controls stringent factors by exploiting antagonistic allosteric coupling between catalytic domains. Molecular cell, 81(16), 3310-3322.e6. doi:10.1016/j.molcel.2021.07.0268.
Takada, H., Roghanian, M., Caballero Montes, J., Van Nerom, K., Jimmy, S., Kudrin, P., Trebini, F., Murayama, R., Akanuma, G., Garcia-Pino, A., & Hauryliuk, V. (2021). Ribosome association primes the stringent factor Rel for tRNA-dependent locking in the A-site and activation of (p)ppGpp synthesis. Nucleic acids research, 49(1), 444-457. doi:10.1093/nar/gkaa11879.
Takada, H., Roghanian, M., Caballero Montes, J., Van Nerom, K., Jimmy, S., Kudrin, P., Trebini, F., Murayama, R., Akanuma, G., Garcia-Pino, A., & Hauryliuk, V. (2021). Ribosome association primes the stringent factor Rel for tRNA-dependent locking in the A-site and activation of (p)ppGpp synthesis. Nucleic acids research, 49(1), 444-457. doi:10.1093/nar/gkaa118710.
Tamman, H., Van Nerom, K., Takada, H., Vandenberk, N., Scholl, D., Polikanov, Y., Hofkens, J., Talavera Perez, A., Hauryliuk, V., Hendrix, J., & Garcia-Pino, A. (2020). A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes. Nature Chemical Biology, 16(8), 834-840. doi:10.1038/s41589-020-0520-2