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Journal Abstract Search


215 related items for PubMed ID: 7961469

  • 1. Carboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation.
    Hou Y, Yaskowiak ES, March PE.
    J Bacteriol; 1994 Nov; 176(22):7038-44. PubMed ID: 7961469
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  • 3. Synthesis of guanosine 5'-di- and -triphosphate derivatives with modified terminal phosphates: effect on ribosome-elongation factor G-dependent reactions.
    Eckstein F, Bruns W, Parmeggiani A.
    Biochemistry; 1975 Nov 18; 14(23):5225-32. PubMed ID: 1103967
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  • 8. Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2.
    Nygård O, Nilsson L.
    Eur J Biochem; 1989 Feb 15; 179(3):603-8. PubMed ID: 2537725
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  • 9. Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome.
    Rodnina MV, Savelsbergh A, Matassova NB, Katunin VI, Semenkov YP, Wintermeyer W.
    Proc Natl Acad Sci U S A; 1999 Aug 17; 96(17):9586-90. PubMed ID: 10449736
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  • 10. Use of the photoactivated analog of elongation factor G for the study of its interaction with ribosomes.
    Girshovich AS, Kurtskhalia TV.
    Methods Enzymol; 1979 Aug 17; 60():719-26. PubMed ID: 459925
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  • 11. An A to U transversion at position 1067 of 23 S rRNA from Escherichia coli impairs EF-Tu and EF-G function.
    Saarma U, Remme J, Ehrenberg M, Bilgin N.
    J Mol Biol; 1997 Sep 26; 272(3):327-35. PubMed ID: 9325093
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  • 13. Release factor RF-3 GTPase activity acts in disassembly of the ribosome termination complex.
    Grentzmann G, Kelly PJ, Laalami S, Shuda M, Firpo MA, Cenatiempo Y, Kaji A.
    RNA; 1998 Aug 26; 4(8):973-83. PubMed ID: 9701288
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  • 15. The elongation factor G carries a catalytic site for GTP hydrolysis, which is revealed by using 2-propanol in the absence of ribosomes.
    De Vendittis E, Masullo M, Bocchini V.
    J Biol Chem; 1986 Apr 05; 261(10):4445-50. PubMed ID: 3007457
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  • 17. The function of conserved amino acid residues adjacent to the effector domain in elongation factor G.
    Sharer JD, Koosha H, Church WB, March PE.
    Proteins; 1999 Nov 01; 37(2):293-302. PubMed ID: 10584074
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  • 18. The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome.
    Vorstenbosch E, Pape T, Rodnina MV, Kraal B, Wintermeyer W.
    EMBO J; 1996 Dec 02; 15(23):6766-74. PubMed ID: 8978702
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