Inhibitory effect of EF G and GMPPCP on peptidyl transferase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(74)81169-5/fullpdf
Reference22 articles.
1. Ribosomes Cannot Interact Simultaneously with Elongation Factors EF Tu and EF G
2. Inhibition by Elongation Factor EF G of Aminoacyl-tRNA Binding to Ribosomes
3. Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes
4. Inability of E. coli ribosomes to interact simultaneously with the bacterial elongation factors EF Tu and EF G
Cited by 5 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. Effect of P and A site substrates on the binding of a macrolide to ribosomes. Analysis of the puromycin-induced stimulation;European Journal of Biochemistry;1984-08
2. Mode of action of bottromycin A2 : effect on peptide bond formation;FEBS Letters;1981-01-26
3. The Genetic Mechanism: II The Cell’s Employment of DNA;The Genetic Mechanism and the Origin of Life;1978
4. Polysomal ribosomes complexed with elongation factor G can engage in the peptidyl transfer reaction;FEBS Letters;1976-10-01
5. Synthesis of guanosine 5'-di- and -triphosphate derivatives with modified terminal phosphates. Effect on ribosome-elongation factor G-dependent reactions;Biochemistry;1975-11
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