Evidence map›Paper›PMID 31473440›Full record

ReviewCurrent opinion in structural biology2019

Dcp2: an mRNA decapping enzyme that adopts many different shapes and forms.

Jan Philip Wurm, Remco Sprangers

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Genome-wide mapping of DCP2-dependent 5' cap footprints inNAR genomics and bioinformatics · 2026
    Article
  2. RNA regulation in plants.Science China. Life sciences · 2026
    Review
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  16. Endoribonuclease DNE1 Promotes Ethylene Response by ModulatingInternational journal of molecular sciences · 2024
    Article
  17. Review
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  19. Assessing the applicability ofJournal of biomolecular NMR · 2023
    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

2 authors.

Jan Philip WurmDepartment of Biophysics I, University of Regensburg, 93053, Regensburg, Germany. Electronic address: jan-philip.wurm@biologie.uni-regensburg.de.
Remco SprangersDepartment of Biophysics I, University of Regensburg, 93053, Regensburg, Germany. Electronic address: remco.sprangers@ur.de.

Funding

European Research Council 616052
6 · The paper itself

Abstract

Eukaryotic mRNAs contain a 5' cap structure that protects the transcript against rapid exonucleolytic degradation. The regulation of cellular mRNA levels therefore depends on a precise control of the mRNA decapping pathways. The major mRNA decapping enzyme in eukaryotic cells is Dcp2. It is regulated by interactions with several activators, including Dcp1, Edc1, and Edc3, as well as by an autoinhibition mechanism. The structural and mechanistical characterization of Dcp2 complexes has long been impeded by the high flexibility and dynamic nature of the enzyme. Here we review recent insights into the catalytically active conformation of the mRNA decapping complex, the mode of action of decapping activators and the large interactions network that Dcp2 is embedded in.

Indexed as

Models, MolecularBinding SitesEndoribonucleasesHumansMolecular ConformationPhase TransitionProtein BindingProtein Interaction MapsRNA CapsRNA, MessengerDCP2 protein, humanEndoribonucleasesmRNA decapping enzymesRNA CapsRNA, Messenger

Identifiers

PMID31473440
PMCPMC6900585

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.