Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes
Author:
Publisher
Pleiades Publishing Ltd
Subject
Structural Biology,Biophysics
Link
http://link.springer.com/content/pdf/10.1134/S0026893308060162.pdf
Reference33 articles.
1. Kisselev L., Ehrenberg M., Frolova L. 2003. Termination of translation: Interplay of mRNA, rRNAs and release factors? EMBO J. 22, 175–182.
2. Song H., Mugnier P., Das A.K., et al. 2000. The crystal structure of human eukaryotic release factor eRF1—mechanism of stop codon recognition and peptidyltRNA hydrolysis. Cell. 100, 311–321.
3. Bertram G., Bell H.A., Ritchie D.W., et al. 2000. Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition. RNA. 6, 1236–1247.
4. Chavatte L., Seit-Nebi A., Dubovaya V., Favre A. 2002. The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. EMBO J. 21, 5302–5311.
5. Frolova L., Seit-Nebi A., Kisselev L. 2002. Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1. RNA. 8, 129–136.
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2. NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor;FEBS Journal;2010-05-11
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