Three Binding Sites for Stalk Protein Dimers Are Generally Present in Ribosomes from Archaeal Organism
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
1. Interaction of the G′ Domain of Elongation Factor G and the C-Terminal Domain of Ribosomal Protein L7/L12 during Translocation as Revealed by Cryo-EM
2. Visualization of elongation factor Tu on the Escherichia coli ribosome
3. Stoichiometry and properties of the complex between ribosomal proteins L7 and L10 in solution
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1. Structural insights into the Switching Off of the Interaction between the Archaeal Ribosomal Stalk and aEF1A by Nucleotide Exchange Factor aEF1B;Journal of Molecular Biology;2021-07
2. Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM;Proceedings of the National Academy of Sciences;2020-12-07
3. Direct visualization of translational GTPase factor-pool formed around the archaeal ribosomal P-stalk by high-speed atomic force microscopy;2020-07-01
4. Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations;Scientific Reports;2019-10-14
5. Structural and Mutagenesis Studies Evince the Role of the Extended Protuberant Domain of Ribosomal Protein uL10 in Protein Translation;Biochemistry;2019-08-16
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