Evidence map›Paper›PMID 40384869›Full record

ReviewInternational journal of biological sciences2025

Control of Snail1 protein stability by post-translational modifications: the basis for a complex regulation of Snail1 function.

Antonio García de Herreros

Abstract readReview
In one paragraph

Review in International journal of biological sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. 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

1 author.

Antonio García de HerrerosPrograma de Recerca en Càncer, Hospital del Mar Research Institute (IMIM), Unidad Asociada al CSIC, Barcelona, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Snail1 transcriptional factor is essential for the epithelial to mesenchymal transition and for the acquisition by tumor cells of properties associated to this transition, such as increased invasion and chemoresistance. Snail1 function is mainly controlled post-translationally, through different modifications that directly or indirectly control Snail1 protein stability. In this review I describe these modifications, the enzymes that produce them and their relevance for Snail1 function, focusing particularly in polyubiquitination and phosphorylation. I also propose several explanations for the divergent effects of some of these modifications, since the phosphorylation of some residues have been reported to both promote and decrease Snail1 stability. Moreover, I discuss the possible causes of the observed Snail1 promiscuity in the interaction with the many factors involved in its regulation, on the basis of the

Indexed as

Protein Processing, Post-TranslationalSnail Family Transcription FactorsTranscription FactorsAnimalsEpithelial-Mesenchymal TransitionHumansPhosphorylationProtein StabilityUbiquitinationSNAI1 protein, humanSnail Family Transcription FactorsTranscription FactorsphosphorylationSnail1Snail1 structureubiquitination

Identifiers

PMID40384869
PMCPMC12080401

What OpenQuestion holds

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LicenceCC BY
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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.