Evidence map›Paper›PMID 32050651›Full record

ReviewCancers2020

Alternative Mechanisms of p53 Action During the Unfolded Protein Response.

Leïla T S Fusée, Mónica Marín, Robin Fåhraeus, Ignacio López

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Growth hormone - releasing hormone in the immune system.Reviews in endocrine & metabolic disorders · 2025
    Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Omics-Based Investigations of Breast Cancer.Molecules (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. The regulatory roles of p53 in cardiovascular health and disease.Cellular and molecular life sciences : CMLS · 2021
    Review
  19. P53 in acute respiratory distress syndrome.Cellular and molecular life sciences : CMLS · 2020
    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 5 countries.

Leïla T S FuséeINSERM U1162, 27 rue Juliette Dodu, 75010 Paris, France.
Mónica MarínBiochemistry-Molecular Biology, Faculty of Science, Universidad de la República, Iguá 4225, Montevideo 11400, Uruguay.
Robin FåhraeusINSERM U1162, 27 rue Juliette Dodu, 75010 Paris, France.
Ignacio LópezBiochemistry-Molecular Biology, Faculty of Science, Universidad de la República, Iguá 4225, Montevideo 11400, Uruguay.
Inserm · FRUniversidad de la República de Uruguay · UY

Funding

Cancerfonden 180296Ministerstvo Školství, Mládeže a Tělovýchovy MEYS - NPS I - LO1413Ministerstvo Zdravotnictví Ceské Republiky MH CZ - DRO (MMCI, 00209805)
6 · The paper itself

Abstract

The tumor suppressor protein p53 orchestrates cellular responses to a vast number of stresses, with DNA damage and oncogenic activation being some of the best described. The capacity of p53 to control cellular events such as cell cycle progression, DNA repair, and apoptosis, to mention some, has been mostly linked to its role as a transcription factor. However, how p53 integrates different signaling cascades to promote a particular pathway remains an open question. One way to broaden its capacity to respond to different stimuli is by the expression of isoforms that can modulate the activities of the full-length protein. One of these isoforms is p47 (p53/47, Δ40p53, p53ΔN40), an alternative translation initiation variant whose expression is specifically induced by the PERK kinase during the Unfolded Protein Response (UPR) following Endoplasmic Reticulum stress. Despite the increasing knowledge on the p53 pathway, its activity when the translation machinery is globally suppressed during the UPR remains poorly understood. Here, we focus on the expression of p47 and we propose that the alternative initiation of p53 mRNA translation offers a unique condition-dependent mechanism to differentiate p53 activity to control cell homeostasis during the UPR. We also discuss how the manipulation of these processes may influence cancer cell physiology in light of therapeutic approaches.

Indexed as

ER stressmRNA translationp47p53UPR

Identifiers

PMID32050651
PMCPMC7072472
OpenAlexW3005068987

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.