Interaction between the Different Domains of Aminoacyl-tRNA and the Elongation-Factor-Tu . Kirromycin Complex
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1983.tb07492.x/fullpdf
Reference45 articles.
1. 1. D. L. Miller, H. Weissbach, H. Weissbach, and S. Petska (1977 ) inMollecular Mechanisms of Protein Biosynthesis () pp.323 -373 , Academic Press, New York.
2. The role of guanosine 5′-triphosphate in polypeptide chain elongation
3. Hydrolysis of GTP by elongation factor Tu can be induced by monovalent cations in the absence of other effectors.
4. Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2
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1. Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity;FEBS Letters;1994-04-18
2. The Synthesis, Reactions, and Properties of the 2′(3′)-O-Aminoacyl and Peptidyl Nucleosides and Nucleotides;Chemistry of Nucleosides and Nucleotides;1994
3. Binding of periodate-oxidized guanine nucleotides to eukaryotic elongation factor 2;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1990-04
4. Structure-function relationships of elongation factor Tu. Isolation and activity of the guanine-nucleotide-binding domain;European Journal of Biochemistry;1989-06
5. TRNA and the guanosine triphosphatase activity of elongation factor Tu;Biochemistry;1989-01-10
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