Fluorescence labeling of an aminoacyl-tRNA at the 3'-end and its interaction with elongation factor Tu·GTP
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(86)81015-8/fullpdf
Reference22 articles.
1. The interaction of guanosine 5′-diphosphate, 2′ (3′)-diphosphate with the bacterial elongation factor Tu
2. Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu
3. Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Recognition of Aminoacyl-tRNAs by Protein Elongation Factors;tRNA;2014-04-30
2. Transient Conformational States of Aminoacyl-tRNA during Ribosome Binding Catalyzed by Elongation Factor Tu;Biochemistry;1994-10-11
3. How many EF-Tu molecules participate in aminocyl-tRNA binding?;Biochimie;1991-07
4. Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.cntdot.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis;Biochemistry;1990-05-08
5. Interaction of elongation factor-Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3' terminus;European Journal of Biochemistry;1989-09
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