Conversion of omnipotent translation termination factor eRF1 into ciliate‐like UGA‐only unipotent eRF1
Author:
Affiliation:
1. Engelhardt Institute of Molecular Biology Vavilov str. 32 119991 Moscow Russia
Publisher
EMBO
Subject
Genetics,Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1093/embo-reports/kvf178
Reference27 articles.
1. Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition
2. [30] Mammalian release factor; in Vitro Assay and Purification
3. A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
4. Functional expression of eukaryotic polypeptide chain release factors 1 and 3 by means of baculovirus/insect cells and complex formation between the factors
5. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
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1. The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center;Nature Chemical Biology;2024-01-03
2. Further analyses on the evolutionary “key‐protist” Halteria (Protista, Ciliophora) based on transcriptomic data;Zoologica Scripta;2019-08-17
3. Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae;The FEBS Journal;2018-12-11
4. ‘Stop’ in protein synthesis is modulated with exquisite subtlety by an extended RNA translation signal;Biochemical Society Transactions;2018-11-12
5. Eukaryotic translational termination efficiency is influenced by the 3′ nucleotides within the ribosomal mRNA channel;Nucleic Acids Research;2018-01-09
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