Articles dans des revues avec comité de lecture (81)
  1. 11. 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.2021.06.005
  2. 12. 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.2021.07.026
  3. 13. 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/gkaa1187
  4. 14. 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/gkaa1187
  5. 15. 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
  6. 16. Jimmy, S., Saha, C. K., Kurata, T., Stavropoulos, C., Oliveira, S. R. A., Koh, A., Cepauskas, A., Takada, H., Rejman, D., Tenson, T., Strahl, H., Garcia-Pino, A., Hauryliuk, V., & Atkinson, G. C. (2020). A widespread toxin−antitoxin system exploiting growth control via alarmone signaling. Proceedings of the National Academy of Sciences of the United States of America, 117(19), 10500-10510. doi:10.1073/pnas.1916617117
  7. 17. 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. doi:10.1038/s41589-020-0520-2
  8. 18. Takada, H., Roghanian, M., Murina, V., Dzhygyr, I., Murayama, R., Akanuma, G., Atkinson, G. C., Garcia-Pino, A., & Hauryliuk, V. (2020). The C-Terminal RRM/ACT Domain Is Crucial for Fine-Tuning the Activation of ‘Long’ RelA-SpoT Homolog Enzymes by Ribosomal Complexes. Frontiers in microbiology, 11, 277. doi:10.3389/fmicb.2020.00277
  9. 19. Manav, M. C., Turnbull, K. J., Jurenas, D., Garcia-Pino, A., Gerdes, K., & Brodersen, D. E. (2019). The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain. Structure, 27(11), 1675-1685.e3. doi:10.1016/j.str.2019.08.008
  10. 20. Van Nerom, K., Tamman, H., Takada, H., Hauryliuk, V., & Garcia-Pino, A. (2019). The Rel stringent factor from Thermus thermophilus: Crystallization and X-ray analysis. Acta Crystallographica Section F:Structural Biology Communications, 75, 561-569. doi:10.1107/S2053230X19010628
  11. 21. Jurenas, D., Van Melderen, L., & Garcia-Pino, A. (2019). Mechanism of regulation and neutralization of the AtaR–AtaT toxin–antitoxin system. Nature Chemical Biology, 15(3), 285-294. doi:10.1038/s41589-018-0216-z
  12. 22. Talavera Perez, A., Tamman, H., Ainelo, A., Konijnenberg, A., Hadži, S., Sobott, F., Garcia-Pino, A., Hõrak, R., & Loris, R. (2019). A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. Nature communications, 10(1), 972. doi:10.1038/s41467-019-08865-z
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