Cooperative unfolding of Escherichia coli ribosome recycling factor originating from its domain–domain interaction and its implication for function
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference41 articles.
1. Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
2. A Posttermination Ribosomal Complex Is the Guanine Nucleotide Exchange Factor for Peptide Release Factor RF3
3. Release of Peptide Promoted by the GGQ Motif of Class 1 Release Factors Regulates the GTPase Activity of RF3
4. Evidence for invivo ribosome recycling, the fourth step in protein biosynthesis
5. Amber mutations in ribosome recycling factors ofEscherichia coliandThermus thermophilus: evidence for C-terminal modulator element
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1. The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G in Staphylococcus aureus;Journal of Biological Chemistry;2020-05
2. Thermal Stability of Thermoanaerobacter tengcongensis Ribosome Recycling Factor;Protein & Peptide Letters;2014-01-31
3. Buffer-Dependent Fragmentation of a Humanized Full-Length Monoclonal Antibody;Journal of Pharmaceutical Sciences;2010-07
4. Structural Insights into Ribosome Recycling Factor Interactions with the 70S Ribosome;Journal of Molecular Biology;2008-03
5. C-terminal effect of Thermoanaerobacter tengcongensis ribosome recycling factor on its activity and conformation changes;Archives of Biochemistry and Biophysics;2007-10
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