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April 1, 1984Journal of Biological ChemistryOpen Access

Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.

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Authors

ALAlan LouieUniversity of California, RiversideNRN. Susan RibeiroUniversity of WashingtonBRBrian R. ReidUniversity of California, Riverside

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Louie et al. (1984) studied this question.

synapsesocial.com/papers/6a71cb6e31a3df824329d16fhttps://doi.org/10.1016/s0021-9258(17)42947-4
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The elongation factor Tu binds aminoacyl-tRNA in the presence of GDP.1982 · 59 citations
  2. 2Interaction of Initiator Met-tRNAfMet (Escherichia coli) and Gly-tRNA1Gly (Staphylococcus epidermidis) with Bacterial Elongation Factor Tu: GTP Complex1981 · 28 citations
  3. 3Inactivation of Tu Factor-Guanosine Triphosphate Recognition and Ribosome-binding Ability by Terminal Oxidation-Reduction of Yeast Phenylalanine Transfer Ribonucleic Acid1972 · 64 citations
  4. 4Structural Requirements for Recognition of Escherichia coli Initiator and Non-Initiator Transfer Ribonucleic Acids by Bacterial T Factor1974 · 90 citations
  5. 5Interaction of elongation factor Tu with 2'(3')-O-aminoacyloligonucleotides derived from the 3' terminus of aminoacyl-tRNA.1975 · 44 citations