Conformational transitions of a tRNA-aminoacyl-tRNA synthetase complex induced by tRNAs bearing different modifications in the 3' terminus
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00588a041
Reference31 articles.
1. Kinetics of conformational changes in tRNAPhe (yeast) as studied by the fluorescence of the y-base and of formycin substituted for the 3'-terminal adenine
2. Factors determining the specificity of the tRNA aminoacylation reaction
3. Non-equivalence of the Sites of Yeast Phenylalanyl-tRNA Synthetase during Catalysis
4. Calorimetric Studies on Melting of tRNAPhe (Yeast)
5. Thermodynamics and kinetics of the interaction of phenylalanine-specific tRNA from yeast with its cognate synthetase as studied by the flourescence of the Y-base
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1. Interaction of aminoacyl-tRNA synthetases with tRNA: General principles and distinguishing characteristics of the high-molecular-weight substrate recognition;Biochemistry (Moscow);2007-03
2. The Crystal Structure of the Ternary Complex of Phenylalanyl-tRNA Synthetase with tRNAPhe and a Phenylalanyl-Adenylate Analogue Reveals a Conformational Switch of the CCA End;Biochemistry;2006-08-15
3. Fluorimetric Study of Yeast tRNAPheCCF in the Complex with Phenylalanyl-tRNA Synthetase;European Journal of Biochemistry;2005-03-03
4. The Catalytic Mechanism of Glutamyl-tRNA Synthetase of Escherichia coli;European Journal of Biochemistry;2005-03-03
5. Accuracy of Protein Biosynthesis: Quasi-species Nature of Proteins and Possibility of Error Catastrophes;Journal of Theoretical Biology;1998-07
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