Activities of guanosine triphosphate analogues in reactions catalyzed by elongation factor Tu and initiation factor 2 of Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference45 articles.
1. Protein Biosynthesis
2. Entry site of formylmethionyl-tRNA
3. The Role of Guanosine Triphosphate Hydrolysis in Elongation Factor Tu-promoted Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes
Cited by 15 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. Interaction Studies Between Elongation Factor Tu and Anthraniloyl-fluorescent Analogues of Guanyl Nucleotides;European Journal of Biochemistry;1995-01
2. Affinity labeling of the GDP/GTP binding site in Thermus thermophilus elongation factor Tu;Biochemistry;1988-12
3. Spin-labelled analogues of GDP and GTP as site-specific reporter groups for guanosine nucleotide-binding proteins;Biochimica et Biophysica Acta (BBA) - General Subjects;1986-10
4. Tubulin polymerization with ATP is mediated through the exchangeable GTP site;Biochimica et Biophysica Acta (BBA) - General Subjects;1986-03
5. Structure-function relationship in Escherichia coli initiation factors. Biochemical and biophysical characterization of the interaction between IF-2 and guanosine nucleotides.;Journal of Biological Chemistry;1985-07
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