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December 1, 1985Journal of Biological ChemistryOpen Access

The rate of cleavage of GTP on the binding of Phe-tRNA.elongation factor Tu.GTP to poly(U)-programmed ribosomes of Escherichia coli.

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Authors

JEJohn F. EcclestonMRC London Institute of Medical SciencesDDDaniel B. DixUniversity of South CarolinaRTRichard ThompsonUniversity of Colorado Boulder

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Eccleston et al. (1985) studied this question.

synapsesocial.com/papers/6a94db1bd1979bcb977c3e2ehttps://doi.org/10.1016/s0021-9258(17)36226-9
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Also Consider

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  1. 1The stereochemical course of the ribosome-dependent GTPase reaction of elongation factor G from Escherichia coli.1981 · 37 citations
  2. 2Characterization of the GTPase reaction of elongation factor Tu. Determination of the stereochemical course in the presence of antibiotic X5108.1982 · 47 citations
  3. 3Accuracy of protein biosynthesis. A kinetic study of the reaction of poly(U)-programmed ribosomes with a leucyl-tRNA2-elongation factor Tu-GTP complex.1982 · 67 citations
  4. 4Protein-bound ATP: properties of a key intermediate of the magnesium-dependent subfragment 1 ATPase from rabbit skeletal muscle1982 · 23 citations
  5. 5The accuracy of protein biosynthesis is limited by its speed: high fidelity selection by ribosomes of aminoacyl-tRNA ternary complexes containing GTP[gamma S]1982 · 106 citations