Publikationen von M. V. Rodnina

Polikanov, Y. S.; Osterman, I. A.; Szal, T.; Tashlitsky, V. N.; Serebryakova, M. V.; Kusochek, P.; Bulkley, D.; Malanicheva, I. A.; Efimenko, T. A.; Efremenkova, O. V. et al.; Konevega, A. L.; Shaw, k.J.; Bogdanov, A. A.; Rodnina, M. V.; Dontsova, O. A.; Mankin, A. S.; Steitz, T. A.; Sergiev, P. V.: Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Molecular Cell 56 (4), S. 531 - 540 (2014)

Rudorf, S.; Thommen, M.; Rodnina, M. V.; Lipowsky, R.: Deducing the kinetics of protein synthesis in vivo from the transition rates measured in vitro. PLoS Computational Biology 10 (10), e1003909 (2014)

Ge, Y.; Draycheva, A.; Bornemann, T.; Rodnina, M. V.; Wintermeyer, W.: Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion. Nature Communications 5, 5263 (2014)

Maracci, C.; Peske, F.; Dannies, E.; Pohl, C.; Rodnina, M. V.: Ribosome-induced tuning of GTP hydrolysis by a translational GTPase. Proceedings of the National Academy of Sciences of the United States of America 111 (40), S. 14418 - 14423 (2014)

Holtkamp, W.; Wintermeyer, W.; Rodnina, M. V.: Synchronous tRNA movements during translocation on the ribosome are orchestrated by elongation factor G and GTP hydrolysis. BioEssays 36 (10), S. 908 - 918 (2014)

Garreau de Loubresse, N.; Prokhorova, I.; Holtkamp, W.; Rodnina, M. V.; Yusupova , G.; Yusupov, M.: Structural basis for the inhibition of the eukaryotic ribosome. Nature 513 (7519), S. 517 - 522 (2014)

Samatova, E. N.; Konevega, A. L.; Wills, N. M.; Atkins, J. F.; Rodnina, M. V.: High-efficiency translational bypassing of non-coding nucleotides specified by mRNA structure and nascent peptide. Nature communications 5, 4459 (2014)

Caliskan, N.; Katunin, V. I.; Belardinelli, R.; Peske, F.; Rodnina, M. V.: Programmed –1 frameshifting by kinetic partitioning during impeded translocation. Cell 157 (7), S. 1619 - 1631 (2014)

Rodnina, M. V.: Properties and evolutionary implications of the heliobacterial genome. Advances in botanical research 66, S. 67 - 97 (2013)

Kuhlenkötter, S.; Wintermeyer, W.; Rodnina, M. V.: Different substrate-dependent transition states in the active site of the ribosome. Nature 476, S. 351 - 354 (2011)

Julian, P.; Milon, P.; Agirrezabala, X.; Lasso, G.; Gil, D.; Rodnina, M. V.; Valle, M.: The cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. PLoS Biology 9 (7), e1001095 (2011)

Mittelstät, J.; Konevega, A. L.; Rodnina, M. V.: Distortion of tRNA upon near-cognate codon recognition on the ribosome. Journal of Biological Chemistry 286 (10), S. 8158 - 8164 (2011)

Rodnina, M. V.; Wintermeyer, W.: The ribosome as a molecular machine: The mechanism of tRNA–mRNA movement in translocation. Biochemical Society Transactions 39, S. 658 - 662 (2011)

Wintermeyer, W.; Rodnina, M. V.: Genauigkeit und Geschwindigkeit der Proteinsynthese. Biospektrum 17 (4), S. 389 - 392 (2011)

Wohlgemuth, I.; Pohl, W.; Rodnina, M. V.: Optimization of speed and accuracy of decoding in translation. The EMBO Journal 29 (21), S. 3701 - 3709 (2010)

Milon, P.; Carotti, M.; Konevega, A. L.; Wintermeyer, W.; Rodnina, M. V.; Gualerzi, C. O.: The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex. EMBO Reports 11 (4), S. 312 - 316 (2010)

Rodnina, M. V.: Protein synthesis meets ABC ATPases: new roles for Rli1/ABCE1. EMBO Reports 11 (3), S. 143 - 144 (2010)

Paleskava, A.; Konevega, A. L.; Rodnina, M. V.: Thermodynamic and kinetic framework of selenocysteyl-tRNA(Sec) recognition by elongation factor SelB. The Journal of Biological Chemistry 285 (5), S. 3014 - 3020 (2010)

Burakovsky, D. E.; Sergiev, P. V.; Steblyanko, M. A.; Kubarenko, A. V.; Konevega, A. L.; Bogdanov, A. A.; Rodnina, M. V.; Dontsova, O. A.: Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination. RNA 16 (9), S. 1848 - 1853 (2010)

Byrne, R. T.; Konevega, A. L.; Rodnina, M. V.; Antson, A. A.: The crystal structure of unmodified tRNA^Phe from Escherichia coli. Nucleic Acids Research 38 (12), S. 4154 - 4162 (2010)