Binding interactions between radiolabeled Escherichia coli elongation factor G and the ribosome.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. Selective chemical modification of Escherichia coli elongation factor G. N-Ethylmaleimide modification of a cysteine essential for nucleotide binding.
2. Interaction of E. coli G Factor with the 50S Ribosomal Subunit
3. Identity of the Ribosomal Proteins Involved in the Interaction with Elongation Factor G
4. Coordinate Inhibition of Elongation Factor G Function and Ribosomal Subunit Association by Antibodies to Several Ribosomal Proteins
5. Inhibition of protein L7/L12 binding to 50 S ribosomal cores by antibodies specific for proteins L6, L10 and L18
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1. Intramolecular Movements in EF-G, Trapped at Different Stages in Its GTP Hydrolytic Cycle, Probed by FRET;Journal of Molecular Biology;2010-04
2. Conformational changes in switch I of EF-G drive its directional cycling on and off the ribosome;The EMBO Journal;2009-06-18
3. Synthetic and binding studies on the calcium binding site I of bovine brain calmodulin;International Journal of Peptide and Protein Research;2009-01-12
4. Precise Alignment of Peptidyl tRNA by the Decoding Center Is Essential for EF-G-Dependent Translocation;Molecular Cell;2008-10
5. Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome;RNA;2007-07-13
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