Evidence map›Paper›PMID 25432955›Full record

ArticleNucleic acids research2015

Elimination of cap structures generated by mRNA decay involves the new scavenger mRNA decapping enzyme Aph1/FHIT together with DcpS.

Valerio Taverniti, Bertrand Séraphin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  7. Review
  8. Processing body (P-body) and its mediators in cancer.Molecular and cellular biochemistry · 2022
    Review
  9. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Article
  17. Molecular mechanism for the inhibition of DXO by adenosine 3',5'-bisphosphate.Biochemical and biophysical research communications · 2018
    Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Valerio TavernitiEquipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de Recherche Scientifique (CNRS) UMR 7104/Institut National de Santé et de Recherche Médicale (INSERM) U964/Université de Strasbourg, 67404 Illkirch, France.
Bertrand SéraphinEquipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de Recherche Scientifique (CNRS) UMR 7104/Institut National de Santé et de Recherche Médicale (INSERM) U964/Université de Strasbourg, 67404 Illkirch, France seraphin@igbmc.fr.
Université de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic 5' mRNA cap structures participate to the post-transcriptional control of gene expression before being released by the two main mRNA decay pathways. In the 3'-5' pathway, the exosome generates free cap dinucleotides (m7GpppN) or capped oligoribonucleotides that are hydrolyzed by the Scavenger Decapping Enzyme (DcpS) forming m7GMP. In the 5'-3' pathway, the decapping enzyme Dcp2 generates m7GDP. We investigated the fate of m7GDP and m7GpppN produced by RNA decay in extracts and cells. This defined a pathway involving DcpS, NTPs and the nucleoside diphosphate kinase for m7GDP elimination. Interestingly, we identified and characterized in vitro and in vivo a new scavenger decapping enzyme involved in m7GpppN degradation. We show that activities mediating cap elimination identified in yeast are essentially conserved in human. Their alteration may contribute to pathologies, possibly through the interference of cap (di)nucleotide with cellular function.

Indexed as

RNA StabilityAcid Anhydride HydrolasesAdenosine TriphosphateBis(5'-adenosyl)triphosphataseDinucleoside PhosphatesEndoribonucleasesGuanosine DiphosphateHEK293 CellsHumansNeoplasm ProteinsN-Glycosyl HydrolasesNucleoside-Diphosphate KinaseRNA Cap AnalogsRNA CapsRNA, MessengerSaccharomyces cerevisiae Proteins7-methyl-diguanosine triphosphate7-methylguanosine 5'-diphosphateAcid Anhydride HydrolasesAdenosine TriphosphateBis(5'-adenosyl)triphosphataseDcpS protein, humanDCS1 protein, S cerevisiaeDinucleoside PhosphatesEndoribonucleasesGuanosine Diphosphatem(7)GMPNeoplasm ProteinsN-Glycosyl HydrolasesNucleoside-Diphosphate KinaseRNA Cap AnalogsRNA CapsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID25432955
PMCPMC4288156
OpenAlexW2106548299

What OpenQuestion holds

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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.