Evidence map›Paper›PMID 31394841›Full record

ArticleCells2019

The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in

Sara Martín-Villanueva, Antonio Fernández-Pevida, Dieter Kressler, Jesús de la Cruz

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. Homeostatic regulation of ribosomal proteins by ubiquitin-independent cotranslational degradation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Review
  8. VpdC is a ubiquitin-activated phospholipase effector that regulatesProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. 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

4 authors at 2 institutions in 2 countries.

Sara Martín-VillanuevaInstituto de Biomedicina de Sevilla, Hospital Universitario Virgen del Rocio/CSIC/Universidad de Sevilla, E-41013 Seville, Spain.
Antonio Fernández-PevidaInstituto de Biomedicina de Sevilla, Hospital Universitario Virgen del Rocio/CSIC/Universidad de Sevilla, E-41013 Seville, Spain.
Dieter KresslerUnit of Biochemistry, Department of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland. dieter.kressler@unifr.ch.
Jesús de la CruzInstituto de Biomedicina de Sevilla, Hospital Universitario Virgen del Rocio/CSIC/Universidad de Sevilla, E-41013 Seville, Spain. jdlcd@us.es.
Instituto de Biomedicina de Sevilla · ESUniversity of Fribourg · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin is a highly conserved small eukaryotic protein. It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal moiety to ribosomal proteins. Understanding the role of the ubiquitin fused to ribosomal proteins becomes relevant, as these proteins are practically invariably eS31 and eL40 in the different eukaryotes. Herein, we used the amenable yeast

Indexed as

Ribosomal ProteinsSaccharomyces cerevisiaeUbiquitinRibosomal ProteinsUbiquitinpre-rRNA processingribosomal protein L40 (eL40)ribosome biogenesistranslationUBI1/2 genesubiquitinyeast

Identifiers

PMID31394841
PMCPMC6721733
OpenAlexW2965361393

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.