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The EMBO Journal|June 1, 1995
Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosomeM V Rodnina, R Fricke, L Kuhn, et al.Molekuliarnaia Biologiia|October 26, 2005
[GTPases of translational apparatus]A V Kubarenko, P V Sergiev, M V RodninaJournal of Molecular Biology|July 13, 2000
Role of domains 4 and 5 in elongation factor G functions on the ribosomeA Savelsbergh, N B Matassova, M V Rodnina, et al.Nature|January 2, 1997
Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosomeM V Rodnina, A Savelsbergh, V I Katunin, et al.Biochemistry|November 4, 1998
Interaction of guanine nucleotides with the signal recognition particle from Escherichia coliJ R Jagath, M V Rodnina, G Lentzen, et al.The Journal of Biological Chemistry|January 8, 2000
Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12A Savelsbergh, D Mohr, B Wilden, et al.The EMBO Journal|December 2, 1996
The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosomeE Vorstenbosch, T Pape, M V Rodnina, et al.The Journal of Biological Chemistry|January 12, 1996
Initial binding of the elongation factor Tu.GTP.aminoacyl-tRNA complex preceding codon recognition on the ribosomeM V Rodnina, T Pape, R Fricke, et al.FEBS Letters|April 11, 1988
Number of tRNA binding sites on 80 S ribosomes and their subunitsM V Rodnina, A V El'skaya, Semenkov YuP, et al.Molecular Cell|September 13, 2000
Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosomeF Peske, N B Matassova, A Savelsbergh, et al.Pageof 5