ArticleJournal of molecular evolution2005
Decoding the decoding region: analysis of eukaryotic release factor (eRF1) stop codon-binding residues.
Article in Journal of molecular evolution, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 33 citations in OpenAlex.
- Specificity of mRNA binding to proteins within the NMD machinery is influenced in cancer.Frontiers in molecular biosciences · 2025Article
- Stop or Not: Genome-Wide Profiling of Reassigned Stop Codons in Ciliates.Molecular biology and evolution · 2023Article
- Origin of the omnipotence of eukaryotic release factor 1.Nature communications · 2017Article
- Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.Scientific reports · 2016Article
- Efficient multisite unnatural amino acid incorporation in mammalian cells via optimized pyrrolysyl tRNA synthetase/tRNA expression and engineered eRF1.Journal of the American Chemical Society · 2014Article
- Two-step model of stop codon recognition by eukaryotic release factor eRF1.Nucleic acids research · 2013Article
- Article
- Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1.Nucleic acids research · 2012Article
- Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Nucleic acids research · 2011Article
- A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.Nucleic acids research · 2011Article
- Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.RNA (New York, N.Y.) · 2010Article
- Tandem stop codons in ciliates that reassign stop codons.Journal of molecular evolution · 2009Article
- Macronuclear genome structure of the ciliate Nyctotherus ovalis: single-gene chromosomes and tiny introns.BMC genomics · 2008Article
- Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.BMC evolutionary biology · 2008Article
- Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Distinct paths to stop codon reassignment by the variant-code organisms Tetrahymena and Euplotes.Molecular and cellular biology · 2006Article
- Amino acid residue doublet propensity in the protein-RNA interface and its application to RNA interface prediction.Nucleic acids research · 2006Article
- The evolutionary origin of a complex scrambled gene.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Invariant amino acids essential for decoding function of polypeptide release factor eRF1.Nucleic acids research · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Peptide synthesis in eukaryotes terminates when eukaryotic release factor 1 (eRF1) binds to an mRNA stop codon and occupies the ribosomal A site. Domain 1 of the eRF1 protein has been implicated in stop codon recognition in a number of experimental studies. In order to further pinpoint the residues of this protein involved in stop codon recognition, we sequenced and compared eRF1 genes from a variety of ciliated protozoan species. We then performed a series of computational analyses to evaluate the conservation, accessibility, and structural environment of each amino acid located in domain 1. With this new dataset and methodology, we were able to identify eight specific amino acid sites important for stop codon recognition and also to propose a set of cooperative paired substitutions that may underlie stop codon reassignment. Our results are more consistent with current experimental data than previously described models.
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.