Evidence map›Paper›PMID 18280239›Full record

ArticleMolecular cell2008

Structural basis of dcp2 recognition and activation by dcp1.

Meipei She, Carolyn J Decker, Dmitri I Svergun, Adam Round, Nan Chen, Denise Muhlrad, Roy Parker, Haiwei Song

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

93 citing papers in PubMed, 148 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. ThemicroPublication biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Assessing the applicability ofJournal of biomolecular NMR · 2023
    Article
  13. Review
  14. Article
  15. Article
  16. Dcp2 C-terminaleLife · 2022
    Article
  17. Article
  18. Article
  19. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  20. Article

33 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

8 authors at 6 institutions in 4 countries.

Meipei SheLaboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, 61 Biopolis Drive, Proteos, 138673 Singapore.
Carolyn J Decker
Dmitri I Svergun
Adam Round
Nan Chen
Denise Muhlrad
Roy Parker
Haiwei Song
Agency for Science, Technology and Research · SGUniversity of Arizona · USA.V. Shubnikov Institute of Crystallography · RUEuropean Molecular Biology Laboratory · DEHoward Hughes Medical Institute · USInstitute of Molecular and Cell Biology · SG

Funding

mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R37 GM045443
6 · The paper itself

Abstract

A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor.

Indexed as

Adenosine TriphosphateAlanineAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionBase SequenceBinding SitesCrystallography, X-RayGlutathione TransferaseModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsAdenosine TriphosphateAlanineDcp1 protein, S pombeDcp2 protein, S pombeGlutathione TransferaseRecombinant Fusion ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID18280239
PMCPMC2323275
OpenAlexW1991329325

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.