Evidence map›Paper›PMID 25446649›Full record

ReviewBiochimie2015

NMD: At the crossroads between translation termination and ribosome recycling.

Alper Celik, Stephanie Kervestin, Allan Jacobson

Abstract readReview
In one paragraph

Review in Biochimie, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. New reporters for monitoring cellular NMD.RNA (New York, N.Y.) · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Neoantigens: promising targets for cancer therapy.Signal transduction and targeted therapy · 2023
    Review
  10. Article
  11. Review
  12. Novel clinical presentation andFrontiers in medicine · 2022
    Article
  13. Article
  14. Therapeutic promise of engineered nonsense suppressor tRNAs.Wiley interdisciplinary reviews. RNA · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 2 countries.

Alper CelikDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, 368 Plantation Street, Worcester, MA 01655-0122, USA.
Stephanie KervestinCNRS FRE3630 Associated with Université Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 75005 Paris, France.
Allan JacobsonDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, 368 Plantation Street, Worcester, MA 01655-0122, USA. Electronic address: allan.jacobson@umassmed.edu.
University of Massachusetts Chan Medical School · USUniversité Paris Cité · FR

Funding

Messenger RNA Metabolism in YeastR37GM027757 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JACOBSON, ALLAN S · 2005 to 2014
$6.3M
MESSENGER RNA METABOLISM IN YEASTR01GM027757 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JACOBSON, ALLAN S · 1985 to 2016
$3.8M
NIGMS NIH HHS R01 GM027757NIGMS NIH HHS R37 GM027757NIGMS NIH HHS R37 GM27757
6 · The paper itself

Abstract

Nonsense-mediated mRNA decay (NMD) is one of three regulatory mechanisms that monitor the cytoplasm for aberrant mRNAs. NMD is usually triggered by premature translation termination codons that arise from mutations, transcription errors, or inefficient splicing, but which also occur in transcripts with alternately spliced isoforms or upstream open reading frames, or in the context of long 3'-UTRs. This surveillance pathway requires detection of the nonsense codon by the eukaryotic release factors (eRF1 and eRF3) and the activities of the Upf proteins, but the exact mechanism by which a nonsense codon is recognized as premature, and the individual roles of the Upf proteins, are poorly understood. In this review, we highlight important differences between premature and normal termination. Based on our current understanding of normal termination and ribosome recycling, we propose a similar mechanism for premature termination events that includes a role for the Upf proteins. In this model, the Upf proteins not only target the mRNA and nascent peptide for degradation, but also assume the role of recycling factors and rescue a ribosome stalled at a premature nonsense codon. The ATPase and helicase activities of Upf1, with the help of Upf2 and Upf3, are thus thought to be the catalytic force in ribosome subunit dissociation and ribosome recycling at an otherwise poorly dissociable termination event. While this model is somewhat speculative, it provides a unified vision for current data and a direction for future research.

Indexed as

Nonsense Mediated mRNA DecayPeptide Chain Termination, TranslationalAnimalsHumansProtein BiosynthesisRibosomesNonsense mediated mRNA decayPremature translational terminationRibosome recycling

Identifiers

PMID25446649
PMCPMC4430455
OpenAlexW2047994831

What OpenQuestion holds

Textmetadata
LicenceTDM
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.