Evidence map›Paper›PMID 28480640›Full record

ReviewProtein science : a publication of the Protein Society2017

Dynamic basis of fidelity and speed in translation: Coordinated multistep mechanisms of elongation and termination.

Arjun Prabhakar, Junhong Choi, Jinfan Wang, Alexey Petrov, Joseph D Puglisi

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Ribosomes: from conserved origin to functional/medical mobility and heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. The roles of structural dynamics in the cellular functions of RNAs.Nature reviews. Molecular cell biology · 2019
    Review
  18. Article
  19. Single-Molecule Fluorescence Applied to Translation.Cold Spring Harbor perspectives in biology · 2019
    Review
  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

5 authors at 1 institution in 1 country.

Arjun PrabhakarDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, 94305.
Junhong ChoiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, 94305.
Jinfan WangDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, 94305.
Alexey PetrovDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, 94305.
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, 94305.
Stanford University · US

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
NIGMS NIH HHS R01 GM051266
6 · The paper itself

Abstract

As the universal machine that transfers genetic information from RNA to protein, the ribosome synthesizes proteins with remarkably high fidelity and speed. This is a result of the accurate and efficient decoding of mRNA codons via multistep mechanisms during elongation and termination stages of translation. These mechanisms control how the correct sense codon is recognized by a tRNA for peptide elongation, how the next codon is presented to the decoding center without change of frame during translocation, and how the stop codon is discriminated for timely release of the nascent peptide. These processes occur efficiently through coupling of chemical energy expenditure, ligand interactions, and conformational changes. Understanding this coupling in detail required integration of many techniques that were developed in the past two decades. This multidisciplinary approach has revealed the dynamic nature of translational control and uncovered how external cellular factors such as tRNA abundance and mRNA modifications affect the synthesis of the protein product. Insights from these studies will aid synthetic biology and therapeutic approaches to translation.

Indexed as

AnimalsCodon, TerminatorHumansPeptide Chain Elongation, TranslationalPeptide Chain Termination, TranslationalRNA, TransferCodon, TerminatorRNA, TransferelongationfidelitymRNAribosometerminationtranslationtRNA

Identifiers

PMID28480640
PMCPMC5477533
OpenAlexW2612235447

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.