Evidence map›Paper›PMID 23353937›Full record

ArticleRNA (New York, N.Y.)2013

Multiple Nudix family proteins possess mRNA decapping activity.

Man-Gen Song, Sophie Bail, Megerditch Kiledjian

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

79 citing papers in PubMed, 153 citations in OpenAlex.

  1. Review
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  5. Role ofZoological research · 2026
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  8. 5'-terminal glycosylation of protein-coding transcripts: An epitranscriptomic modification that prolongs mRNA lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Application of Mammalian Nudix Enzymes to Capped RNA Analysis.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. RSC chemical biology · 2023
    Article
  19. Article
  20. Article

19 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Man-Gen SongDepartment of Cell Biology and Neuroscience, Rutgers University, Piscataway, New Jersey 08854-8082, USA.
Sophie Bail
Megerditch Kiledjian
Rutgers, The State University of New Jersey · US

Funding

Regulation of Mammalian mRNA DecayR01GM067005 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KILEDJIAN, MEGERDITCH · 2004 to 2022
$5.5M
NIGMS NIH HHS GM67005NIGMS NIH HHS R01 GM067005
6 · The paper itself

Abstract

RNA decapping is an important contributor to gene expression and is a critical determinant of mRNA decay. The recent demonstration that mammalian cells harbor at least two distinct decapping enzymes that preferentially modulate a subset of mRNAs raises the intriguing possibility of whether additional decapping enzymes exist. Because both known decapping proteins, Dcp2 and Nudt16, are members of the Nudix hydrolase family, we set out to determine whether other members of this family of proteins also contain intrinsic RNA decapping activity. Here we demonstrate that six additional mouse Nudix proteins--Nudt2, Nudt3, Nudt12, Nudt15, Nudt17, and Nudt19--have varying degrees of decapping activity in vitro on both monomethylated and unmethylated capped RNAs. The decapping products from Nudt17 and Nudt19 were analogous to Dcp2 and predominantly generated m⁷GDP, while cleavage by Nudt2, Nudt3, Nudt12, and Nudt15 was more pleiotropic and generated both m⁷GMP and m⁷GDP. Interestingly, all six Nudix proteins as well as both Dcp2 and Nudt16 could hydrolyze the cap of an unmethylated capped RNA, indicating that decapping enzymes may be less constrained for the presence of the methyl moiety. Investigation of Saccharomyces cerevisiae Nudix proteins revealed that the yeast homolog of Nudt3, Ddp1p, also possesses decapping activity in vitro. Moreover, the bacterial Nudix pyrophosphohydrolase RppH displayed RNA decapping activity and released m⁷GDP product comparable to Dcp2, indicating that decapping is an evolutionarily conserved activity that preceded mammalian cap formation. These findings demonstrate that multiple Nudix family hydrolases may function in mRNA decapping and mRNA stability.

Indexed as

RNA StabilityAnimalsEndoribonucleasesMiceNudix HydrolasesPyrophosphatasesRNA CapsRNA, MessengerSaccharomyces cerevisiaeEndoribonucleasesmRNA decapping enzymesNudix HydrolasesPyrophosphatasesRNA CapsRNA, Messenger

Identifiers

PMID23353937
PMCPMC3677249
OpenAlexW2152823953

What OpenQuestion holds

Textmetadata
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.