2‘-Versus 3‘-OH specificity in tRNA aminoacylation. Further support for the “secondary cognition” proposal.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference35 articles.
1. Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine.
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3. Initial position of aminoacylation of individual Escherichia coli, yeast, and calf liver transfer RNAs
4. Amino acids are not all initially attached to the same position on transfer RNA molecules.
5. Enzymic acylation of oxdized-reduced transfer ribonucleic acid by Escherichia coli, yeast, and rat liver synthetases occurs almost exclusively at the 2'-hydroxyl
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1. Aminoacyl-tRNA-Synthetasen: Einteilung in zwei Klassen durch Chemie an Substraten und Enzymen vorweggenommen;Angewandte Chemie;1993-02
2. Ribosomal binding and dipeptide formation by misacylated tRNAPhe's;Biochemistry;1988-09
3. A carbene-yielding amino acid for incorporation into peptide photoaffinity reagents;Analytical Biochemistry;1985-01
4. Origin of the genetic code and specificity of tRNA aminoacylation. A testable model;Origins of Life;1984
5. Loss of positional specificity in the aminoacylation of Escherichia coli tRNAGly.;Journal of Biological Chemistry;1983-10
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