Neutron-scattering studies of the binding of initiator tRNAMet to Escherichia coli trypsin-modified methionyl-tRNA synthetase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference38 articles.
1. The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. 1. Fluorescence Studies on tRNAMet Binding as a Function of Ligands, Ions and pH
2. The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. Mechanism of the Amino-Acid Activation Reaction Catalyzed by the Native and the Trypsin-Modified Enzymes
3. Antico-operative binding of bacterial and mammalian initiator tRNAMet to methionyl-tRNA synthetase from Escherichia coli
4. Transfer RNA: Structure, Properties and Recognition;Blanquet,1979
5. Modification of Methionyl-tRNA Synthetase by Proteolytic Cleavage and Properties of the Trypsin-Modified Enzyme
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2. Three-Dimensional Structure of Methionyl-tRNA Synthetase from Pyrococcus abyssi,;Biochemistry;2004-02-10
3. Detection of Noncovalent tRNA·Aminoacyl-tRNA Synthetase Complexes by Matrix-assisted Laser Desorption/Ionization Mass Spectrometry;Journal of Biological Chemistry;1997-12
4. Critical Role of the Acceptor Stem of tRNAsMet in their Aminoacylation by Escherichia coli Methionyl-tRNA Synthetase;Journal of Molecular Biology;1993-01
5. Evidence for two types of complexes formed by yeast tyrosyl-tRNA synthetase with cognate and non-cognate tRNA. Effect of ribonucleoside triphosphates;European Journal of Biochemistry;1990-11
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