Evidence map›Paper›PMID 32817446›Full record

ArticleRNA (New York, N.Y.)2020

Termi-Luc: a versatile assay to monitor full-protein release from ribosomes.

Denis Susorov, Shawn Egri, Andrei A Korostelev

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. eLife · 2026
    Article
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  6. Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
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  11. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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 1 institution in 1 country.

Denis SusorovRNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
Shawn EgriRNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
Andrei A KorostelevRNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
University of Massachusetts Chan Medical School · US

Funding

Translational Control: Discovery and MechanismsR35GM127094 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Andrei Korostelev · 2018 to 2026
$5.5M
Structural bases for cellular stress responses mediated by stalled translationR01GM106105 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2013 to 2017
$1.6M
Molecular principles of translation terminationR01GM107465 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2015 to 2018
$1.3M
NIGMS NIH HHS R01 GM106105NIGMS NIH HHS R01 GM107465NIGMS NIH HHS R35 GM127094
6 · The paper itself

Abstract

Termination of protein biosynthesis is an essential step of gene expression, during which a complete functional protein is released from the ribosome. Premature or inefficient termination results in truncated, nonfunctional, or toxic proteins that may cause disease. Indeed, more than 10% of human genetic diseases are caused by nonsense mutations leading to premature termination. Efficient and sensitive approaches are required to study eukaryotic termination mechanisms and to identify potential therapeutics that modulate termination. Canonical radioactivity-based termination assays are complex, report on a short peptide release, and are incompatible with high-throughput screening. Here we describe a robust and simple in vitro assay to study the kinetics of full-protein release. The assay monitors luminescence upon release of nanoluciferase from a mammalian pretermination complex. The assay can be used to record time-progress curves of protein release in a high-throughput format, making it optimal for studying release kinetics and for high-throughput screening for small molecules that modulate the efficiency of termination.

Indexed as

Protein BiosynthesisBiological AssayHumansLuciferasesPeptide Chain Termination, TranslationalPeptide Termination FactorsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLuciferasesPeptide Termination FactorsSaccharomyces cerevisiae Proteinsluminescenceprotein releasetranslation termination

Identifiers

PMID32817446
PMCPMC7668252
OpenAlexW3049410494

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.