Evidence map›Paper›PMID 8643594›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis.

K Ito, K Ebihara, M Uno, Y Nakamura

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 136 citations in OpenAlex.

  1. Translation in Mitochondrial Ribosomes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  2. Article
  3. Article
  4. Origins and Early Evolution of the tRNA Molecule.Life (Basel, Switzerland) · 2015
    Review
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  18. Evolutionary conservation of reactions in translation.Microbiology and molecular biology reviews : MMBR · 2002
    Review
  19. Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

K ItoDepartment of Tumor Biology, Institute of Medical Science, University of Tokyo, Japan.
K Ebihara
M Uno
Y Nakamura
The University of Tokyo · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translation termination requires two codon-specific polypeptide release factors in prokaryotes and one omnipotent factor in eukaryotes. Sequences of 17 different polypeptide release factors from prokaryotes and eukaryotes were compared. The prokaryotic release factors share residues split into seven motifs. Conservation of many discrete, perhaps critical, amino acids is observed in eukaryotic release factors, as well as in the C-terminal portion of elongation factor (EF) G. Given that the C-terminal domains of EF-G interacts with ribosomes by mimicry of a tRNA structure, the pattern of conservation of residues in release factors may reflect requirements for a tRNA-mimicry for binding to the A site of the ribosome. This mimicry would explain why release factors recognize stop codons and suggests that all prokaryotic and eukaryotic release factors evolved from the progenitor of EF-G.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBacteriaConserved SequenceFungal ProteinsHumansModels, BiologicalModels, StructuralMolecular Sequence DataNucleic Acid ConformationPeptide Chain Termination, TranslationalPeptide Elongation Factor GPeptide Elongation FactorsPeptide Termination FactorsProtein ConformationFungal ProteinsPeptide Elongation Factor GPeptide Elongation FactorsPeptide Termination FactorsRNA, TransferRNA, Transfer, PheSaccharomyces cerevisiae ProteinsSUP45 protein, S cerevisiae

Identifiers

PMID8643594
PMCPMC39265
OpenAlexW2064735659

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.