Evidence map›Paper›PMID 23354061›Full record

ReviewCellular and molecular life sciences : CMLS2013

The translational factor eIF3f: the ambivalent eIF3 subunit.

Roberta Marchione, Serge A Leibovitch, Jean-Luc Lenormand

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  7. Structures of MPND Reveal the Molecular Recognition of Nucleosomes.International journal of molecular sciences · 2023
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  19. Maternal Dead-end 1 promotes translation ofDevelopment (Cambridge, England) · 2017
    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 2 institutions in 2 countries.

Roberta MarchioneHumProTher Laboratory, TheREx, TIMC-IMAG Laboratory, CNRS UMR5525, University Joseph Fourier, 38700, La Tronche, Cedex, France.
Serge A Leibovitch
Jean-Luc Lenormand
Centre National de la Recherche Scientifique · FRInstitut National de la Recherche Agronomique · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The regulation of the protein synthesis has a crucial role in governing the eukaryotic cell growth. Subtle changes of proteins involved in the translation process may alter the rate of the protein synthesis and modify the cell fate by shifting the balance from normal status into a tumoral or apoptotic one. The largest eukaryotic initiation factor involved in translation regulation is eIF3. Amongst the 13 factors constituting eIF3, the f subunit finely regulates this balance in a cell-type-specific manner. Loss of this factor causes malignancy in several cells, and atrophy in normal muscle cells. The intracellular interacting partners which influence its physiological significance in both cancer and muscle cells are detailed in this review. By delineating the global interaction network of this factor and by clarifying its intracellular role, it becomes apparent that the f subunit represents a promising candidate molecule to use for biotherapeutic applications.

Indexed as

Eukaryotic Initiation Factor-3HumansMuscle CellsNeoplasmsProtein BiosynthesisProtein SubunitsEukaryotic Initiation Factor-3Protein Subunits

Identifiers

PMID23354061
PMCPMC3771369
OpenAlexW2165194174

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.