Both positional isomers of aminoacyl-tRNA's are bound by elongation factor Tu.

This publication has 40 references indexed in Scilit:

• 2‘-Versus 3‘-OH specificity in tRNA aminoacylation. Further support for the “secondary cognition” proposal.
  Published by Elsevier ,1978
• Initial position of aminoacylation of individual Escherichia coli, yeast, and calf liver transfer RNAs
  Biochemistry, 1977
• Participation of isomeric tRNA'S in the partial reactions of protein biosynthesis
  Tetrahedron, 1977
• Hydrolytic action of aminoacyl-tRNA synthetases from Baker's yeast: "chemical proofreading" preventing acylation of tRNA^Ile with misactivated valine
  Biochemistry, 1976
• Position of aminoacylation of individual Escherichia coli and yeast tRNAs.
  Proceedings of the National Academy of Sciences, 1976
• Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine.
  Proceedings of the National Academy of Sciences, 1975
• Amino acids are not all initially attached to the same position on transfer RNA molecules.
  Proceedings of the National Academy of Sciences, 1975
• Chemical Studies on Amino Acid Acceptor Ribonucleic Acids. IV. Position of the Amino Acid Residue in Aminoacyl S-RNA: Chemical Approach^*
  Biochemistry, 1965
• On the Site of Esterification of Amino Acids to Soluble RNA^*
  Biochemistry, 1964
• Chemical evidence for the 3′-linkage of amino acids to S-RNA
  Biochemical and Biophysical Research Communications, 1964