Transfer ribonucleic acid deprived of the C-C-A 3'-extremity can interact with elongation factor Tu
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00288a009
Reference36 articles.
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2. Conformational Activation of Aminoacyl-tRNA Synthetases upon Binding of tRNA. A Facet of a Multi-Step Adaptation Process Leading to the Optimal Biological Activity
3. Stimulation of Escherichia Coli elongation factor Tu-dependent GTP hydrolysis by aminoacyl oligonucleotides in the presence of aurodox
4. Elongation factor Tu.ribosome dependent GTP hydrolysis: elucidation of the role of the AA-tRNA 3' terminus and site(s) involved in the inducing of the GTPase reaction
5. A study of the interaction of Escherichia coli elongation factor-Tu with aminoacyl-tRNAs by partial digestion with cobra venom ribonuclease
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1. EF-Tu from the enacyloxin producing Frateuria W-315 strain: Structure/activity relationship and antibiotic resistance;Biochimie;2016-08
2. Mechanisms of EF-Tu, a pioneer GTPase;Progress in Nucleic Acid Research and Molecular Biology;2002
3. Functional-Structural Analysis of Threonine 25, a Residue Coordinating the Nucleotide-bound Magnesium in Elongation Factor Tu;Journal of Biological Chemistry;1999-04
4. EF-Tu, a GTPase odyssey;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1998-11
5. The Elongation Phase of Protein Synthesis;Progress in Nucleic Acid Research and Molecular Biology;1996
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