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Journal Abstract Search

119 related items for PubMed ID: 3071682

  • 1. Quantitative indicator assay of tRNA binding to the ribosomal P and A sites.
    Lill R, Wintermeyer W.
    Methods Enzymol; 1988; 164():597-611. PubMed ID: 3071682
    [No Abstract] [Full Text] [Related]

  • 2. GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs.
    Rodnina MV, Wintermeyer W.
    Proc Natl Acad Sci U S A; 1995 Mar 14; 92(6):1945-9. PubMed ID: 7892205
    [Abstract] [Full Text] [Related]

  • 3. Time-resolved fluorescence studies on the ternary complex formed between bacterial elongation factor Tu, guanosine 5'-triphosphate, and phenylalanyl-tRNAPhe.
    Hazlett TL, Johnson AE, Jameson DM.
    Biochemistry; 1989 May 02; 28(9):4109-17. PubMed ID: 2665814
    [Abstract] [Full Text] [Related]

  • 4. Undecagold cluster modified tRNA(Phe) from Escherichia coli and its activity in the protein elongation cycle.
    Blechschmidt B, Shirokov V, Sprinzl M.
    Eur J Biochem; 1994 Jan 15; 219(1-2):65-71. PubMed ID: 8307030
    [Abstract] [Full Text] [Related]

  • 5. Apparent association constants of tRNAs for the ribosomal A, P, and E sites.
    Schilling-Bartetzko S, Franceschi F, Sternbach H, Nierhaus KH.
    J Biol Chem; 1992 Mar 05; 267(7):4693-702. PubMed ID: 1537852
    [Abstract] [Full Text] [Related]

  • 6. Parameters for the preparation of Escherichia coli ribosomes and ribosomal subunits active in tRNA binding.
    Rheinberger HJ, Geigenmüller U, Wedde M, Nierhaus KH.
    Methods Enzymol; 1988 Mar 05; 164():658-70. PubMed ID: 3071687
    [No Abstract] [Full Text] [Related]

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  • 8. Mutagenesis of glutamine 290 in Escherichia coli and mitochondrial elongation factor Tu affects interactions with mitochondrial aminoacyl-tRNAs and GTPase activity.
    Hunter SE, Spremulli LL.
    Biochemistry; 2004 Jun 08; 43(22):6917-27. PubMed ID: 15170329
    [Abstract] [Full Text] [Related]

  • 9. The rate of cleavage of GTP on the binding of Phe-tRNA.elongation factor Tu.GTP to poly(U)-programmed ribosomes of Escherichia coli.
    Eccleston JF, Dix DB, Thompson RC.
    J Biol Chem; 1985 Dec 25; 260(30):16237-41. PubMed ID: 3905812
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  • 12. Aminoacyl-tRNA-elongation factor Tu-ribosome interaction leading to hydrolysis of guanosine 5'-triphosphate.
    Takahashi K, Ghag S, Chládek S.
    Biochemistry; 1986 Dec 16; 25(25):8330-6. PubMed ID: 3545292
    [Abstract] [Full Text] [Related]

  • 13. 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
    [Abstract] [Full Text] [Related]

  • 14. Binding of aminoacyl-tRNA to ribosomes promoted by elongation factor Tu. Studies on the role of GTP hydrolysis.
    Yokosawa H, Kawakita M, Arai K, Inoue-Yokosawa N, Kaziro Y.
    J Biochem; 1975 Apr 02; 77(4):719-28. PubMed ID: 1097432
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  • 15. tRNA binding sites on the subunits of Escherichia coli ribosomes.
    Gnirke A, Nierhaus KH.
    J Biol Chem; 1986 Nov 05; 261(31):14506-14. PubMed ID: 3533922
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  • 16. Photoaffinity labeling of peptidyltransferase.
    Kuechler E, Steiner G, Barta A.
    Methods Enzymol; 1988 Nov 05; 164():361-72. PubMed ID: 2468067
    [No Abstract] [Full Text] [Related]

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  • 18. Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu.
    Wolf H, Chinali G, Parmeggiani A.
    Proc Natl Acad Sci U S A; 1974 Dec 05; 71(12):4910-4. PubMed ID: 4373734
    [Abstract] [Full Text] [Related]

  • 19. Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation.
    Nazarenko IA, Harrington KM, Uhlenbeck OC.
    EMBO J; 1994 May 15; 13(10):2464-71. PubMed ID: 8194535
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  • 20. How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?
    Ehrenberg M, Rojas AM, Weiser J, Kurland CG.
    J Mol Biol; 1990 Feb 20; 211(4):739-49. PubMed ID: 2179565
    [Abstract] [Full Text] [Related]

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