Evidence map›Paper›PMID 12218187›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

The hDcp2 protein is a mammalian mRNA decapping enzyme.

Zuoren Wang, Xinfu Jiao, Anne Carr-Schmid, Megerditch Kiledjian

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 209 papers.

0numbers the graph read from it
0cells of the map it votes in
209citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

209 citing papers in PubMed, 330 citations in OpenAlex.

  1. Genome-wide mapping of DCP2-dependent 5' cap footprints inNAR genomics and bioinformatics · 2026
    Article
  2. Review
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  8. Article
  9. Uridine as a hub in cancer metabolism and RNA biology.Experimental & molecular medicine · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Application of Mammalian Nudix Enzymes to Capped RNA Analysis.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  19. Photoactivatable mRNA 5' Cap Analogs for RNA-Protein Crosslinking.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Zuoren WangDepartment of Cell Biology and Neuroscience, Rutgers University, 604 Allison Road, Piscataway, NJ 08854-8082, USA.
Xinfu Jiao
Anne Carr-Schmid
Megerditch Kiledjian
Rutgers, The State University of New Jersey · US

Funding

RNA/PROTEIN INTERACTIONS REGULATING MRNA STABILITYR01DK051611 · NIDDK · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KILEDJIAN, MEGERDITCH · 1997 to 2006
$1.8M
NIDDK NIH HHS DK51611NIDDK NIH HHS R01 DK051611
6 · The paper itself

Abstract

Decapping of mRNA is a critical step in eukaryotic mRNA turnover, yet the proteins involved in this activity remain elusive in mammals. We identified the human Dcp2 protein (hDcp2) as an enzyme containing intrinsic decapping activity. hDcp2 specifically hydrolyzed methylated capped RNA to release m(7)GDP; however, it did not function on the cap structure alone. hDcp2 is therefore functionally distinct from the recently identified mammalian scavenger decapping enzyme, DcpS. hDcp2-mediated decapping required a functional Nudix (nucleotide diphosphate linked to an X moiety) pyrophosphatase motif as mutations in conserved amino acids within this motif disrupted the decapping activity. hDcp2 is detected exclusively in the cytoplasm and predominantly cosediments with polysomes. Consistent with the localization of hDcp2, endogenous Dcp2-like decapping activity was detected in polysomal fractions prepared from mammalian cells. Similar to decapping in yeast, the presence of the poly(A) tail was inhibitory to the endogenous decapping activity, yet unlike yeast, competition of cap-binding proteins by cap analog did not influence the efficiency of decapping. Therefore the mammalian homologue of the yeast Dcp2 protein is an mRNA decapping enzyme demonstrated to contain intrinsic decapping activity.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid MotifsBinding, CompetitiveBlotting, WesternChromatography, Thin LayerCloning, MolecularCytoplasmDNA, ComplementaryElectrophoresis, Polyacrylamide GelEndoribonucleasesFungal ProteinsHumansK562 CellsMolecular Sequence DataNudix HydrolasesPlasmidsDCP2 protein, humanDCP2 protein, S cerevisiaeDNA, ComplementaryEndoribonucleasesFungal ProteinsNPY1 protein, S cerevisiaeNudix HydrolasesPoly APyrophosphatasesRecombinant ProteinsRNARNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID12218187
PMCPMC130517
OpenAlexW2031345354

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.