The binding site for the 3′-terminus of aminoacyl-tRNA in the molecule of elongation factor TufromEscherichia coli
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(79)80210-0/fullpdf
Reference21 articles.
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4. On three complementary amino acid polymerization factors from Bacillus stearothermophilus: separation of a complex containing two of the factors, guanosine-5'-triphosphate and aminoacyl-transfer RNA.
5. Interaction of elongation factor Tu with 2'(3')-O-aminoacyloligonucleotides derived from the 3' terminus of aminoacyl-tRNA.
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1. Effects of Antibiotics, N-Acetylaminoacyl-tRNA and Other Agents on the Elongation-Factor-Tu Dependent and Ribosome-Dependent GTP Hydrolysis Promoted by 2′(3′)-O-l-Phenylalanyladenosine;European Journal of Biochemistry;2005-03-03
2. Specific Recognition of a Minimal Model of Aminoacylated tRNA by the Elongation Factor Tu of Bacterial Protein Biosynthesis;Angewandte Chemie International Edition in English;1997-12-01
3. Molekulare Erkennung eines Minimalmodells der aminoacylierten tRNA durch den Elongationsfaktor Tu der bakteriellen Proteinbiosynthese;Angewandte Chemie;1997-11-14
4. Interaction of N-Tosyl-l-Phenylalanylchloromethane with Thermus Thermophilus Elongation Factor Tu;European Journal of Biochemistry;1997-07
5. Site-directed mutagenesis of elongation factor Tu. The functional and structural role of residue Cys81;European Journal of Biochemistry;1992-09
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