ArticleNucleic acids research2013
Two-step model of stop codon recognition by eukaryotic release factor eRF1.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 63 citations in OpenAlex.
- RNAViruses · 2026Review
- Eukaryotic initiation factor eIF3 facilitates loading of eukaryotic release factor eRF1 or suppressor tRNA to the ribosome.Nucleic acids research · 2026Article
- High throughput screening of eukaryotic release factor 1 variants to enhance noncanonical amino acid incorporation.bioRxiv : the preprint server for biology · 2025Article
- Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation.Nucleic acids research · 2025Article
- Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024Article
- The impact of mRNA poly(A) tail length on eukaryotic translation stages.Nucleic acids research · 2024Article
- Identification of a non-canonical ciliate nuclear genetic code where UAA and UAG code for different amino acids.PLoS genetics · 2023Article
- Features and factors that dictate if terminating ribosomes cause or counteract nonsense-mediated mRNA decay.The Journal of biological chemistry · 2022Review
- Multiplex base editing to convert TAG into TAA codons in the human genome.Nature communications · 2022Article
- Nsp1 of SARS-CoV-2 stimulates host translation termination.RNA biology · 2021Article
- Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.Biochemistry. Biokhimiia · 2021Review
- Article
- eRF1 mediates codon usage effects on mRNA translation efficiency through premature termination at rare codons.Nucleic acids research · 2019Article
- Two classes of EF1-family translational GTPases encoded by giant viruses.Nucleic acids research · 2019Article
- Polyadenylate-binding protein-interacting proteins PAIP1 and PAIP2 affect translation termination.The Journal of biological chemistry · 2019Article
- Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae.The FEBS journal · 2019Article
- Article
- Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Mechanism of premature translation termination on a sense codon.The Journal of biological chemistry · 2018Article
- Origin of the omnipotence of eukaryotic release factor 1.Nature communications · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Release factor eRF1 plays a key role in the termination of protein synthesis in eukaryotes. The eRF1 consists of three domains (N, M and C) that perform unique roles in termination. Previous studies of eRF1 point mutants and standard/variant code eRF1 chimeras unequivocally demonstrated a direct involvement of the highly conserved N-domain motifs (NIKS, YxCxxxF and GTx) in stop codon recognition. In the current study, we extend this work by investigating the role of the 41 invariant and conserved N-domain residues in stop codon decoding by human eRF1. Using a combination of the conservative and non-conservative amino acid substitutions, we measured the functional activity of >80 mutant eRF1s in an in vitro reconstituted eukaryotic translation system and selected 15 amino acid residues essential for recognition of different stop codon nucleotides. Furthermore, toe-print analyses provide evidence of a conformational rearrangement of ribosomal complexes that occurs during binding of eRF1 to messenger RNA and reflects stop codon decoding activity of eRF1. Based on our experimental data and molecular modelling of the N-domain at the ribosomal A site, we propose a two-step model of stop codon decoding in the eukaryotic ribosome.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.