Evidence map›Paper›PMID 18678652›Full record

ArticleMolecular and cellular biology2008

Crystal structure of human Edc3 and its functional implications.

Sharon H M Ling, Carolyn J Decker, Martin A Walsh, Meipei She, Roy Parker, Haiwei Song

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

49 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Global Discovery of Covalent Modulators of Ribonucleoprotein Granules.Journal of the American Chemical Society · 2023
    Article
  7. Review
  8. Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Synthesis of 2-Oxoquinoline Derivatives as Dual Pim and mTORC Protein Kinase Inhibitors.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2022
    Article
  11. Article
  12. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

6 authors at 3 institutions in 3 countries.

Sharon H M LingLaboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673, Singapore.
Carolyn J Decker
Martin A Walsh
Meipei She
Roy Parker
Haiwei Song
Institute of Macromolecular Chemistry · UAHoward Hughes Medical Institute · USMangalam Research Center for Buddhist Languages · US

Funding

Howard Hughes Medical InstituteMedical Research Council G0500367
6 · The paper itself

Abstract

Edc3 is an enhancer of decapping and serves as a scaffold that aggregates mRNA ribonucleoproteins together for P-body formation. Edc3 forms a network of interactions with the components of the mRNA decapping machinery and has a modular domain architecture consisting of an N-terminal Lsm domain, a central FDF domain, and a C-terminal YjeF-N domain. We have determined the crystal structure of the N-terminally truncated human Edc3 at a resolution of 2.2 A. The structure reveals that the YjeF-N domain of Edc3 possesses a divergent Rossmann fold topology that forms a dimer, which is supported by sedimentation velocity and sedimentation equilibrium analysis in solution. The dimerization interface of Edc3 is highly conserved in eukaryotes despite the overall low sequence homology across species. Structure-based site-directed mutagenesis revealed dimerization is required for efficient RNA binding, P-body formation, and likely for regulating the yeast Rps28B mRNA as well, suggesting that the dimeric form of Edc3 is a structural and functional unit in mRNA degradation.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayDimerizationHumansModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNASequence AlignmentEDC3 protein, humanRibonucleoproteins, Small NuclearRNA

Identifiers

PMID18678652
PMCPMC2547010
OpenAlexW2105945357

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.