Publications

Found 10 results
Filters: First Letter Of Last Name is G and Author is Gagnon, Matthieu G  [Clear All Filters]
2025
Aleksandrova, E. V., Syroegin, E. A., Basu, R. S., Vassilevski, A. A., Gagnon, M. G., and Polikanov, Y. S. (2025) Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome. Science. 388, eads9030
2023
Paranjpe, M. N., Marina, V. I., Grachev, A. A., Maviza, T. P., Tolicheva, O. A., Paleskava, A., Osterman, I. A., Sergiev, P. V., Konevega, A. L., Polikanov, Y. S., and Gagnon, M. G. (2023) Insights into the molecular mechanism of translation inhibition by the ribosome-targeting antibiotic thermorubin.. Nucleic Acids Res. 51, 449-462
Seely, S. M., Parajuli, N. P., De Tarafder, A., Ge, X., Sanyal, S., and Gagnon, M. G. (2023) Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome. Nat Commun. 14, 4666
2020
Zhou, D., Tanzawa, T., Lin, J., and Gagnon, M. G. (2020) Structural basis for ribosome recycling by RRF and tRNA. Nat Struct Mol Biol. 27, 25-32
2016
Gagnon, M. G., Lin, J., and Steitz, T. A. (2016) Elongation factor 4 remodels the A-site tRNA on the ribosome. Proc Natl Acad Sci U S A. 113, 4994-9
Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., and Steitz, T. A. (2016) Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res. 44, 2439-50
2015
Lin, J., Gagnon, M. G., Bulkley, D., and Steitz, T. A. (2015) Conformational changes of elongation factor G on the ribosome during tRNA translocation. Cell. 160, 219-27
Roy, R. N., Lomakin, I. B., Gagnon, M. G., and Steitz, T. A. (2015) The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Nat Struct Mol Biol. 22, 466-9
2014
Gagnon, M. G., Lin, J., Bulkley, D., and Steitz, T. A. (2014) Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science. 345, 684-7
2012
Gagnon, M. G., Seetharaman, S. V., Bulkley, D., and Steitz, T. A. (2012) Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science. 335, 1370-2