Evidence map›Paper›PMID 24739740›Full record

ReviewNature reviews. Molecular cell biology2014

DEP domains: structurally similar but functionally different.

Sarah V Consonni, Madelon M Maurice, Johannes L Bos

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2014. 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
–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

49 citing papers in PubMed.

  1. Article
  2. Large-scale functional annotation establishes a reference framework for humanmedRxiv : the preprint server for health sciences · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. The role of kinesin superfamily proteins in hepatocellular carcinoma.Medical oncology (Northwood, London, England) · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Rgs1 is a regulator of effector gene expression during plant infection by the rice blast fungusProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Review
  14. Pathogens (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Skeletal diseases caused by mutations inFrontiers in cell and developmental biology · 2022
    Article
  20. Article
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.

Sarah V ConsonniMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, Utrecht, The Netherlands.
Madelon M MauriceDepartment of Cell Biology, Center for Molecular Medicine, University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands.
Johannes L BosMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, Utrecht, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Dishevelled, EGL-10 and pleckstrin (DEP) domain is a globular protein domain that is present in about ten human protein families with well-defined structural features. A picture is emerging that DEP domains mainly function in the spatial and temporal control of diverse signal transduction events by recruiting proteins to the plasma membrane. DEP domains can interact with various partners at the membrane, including phospholipids and membrane receptors, and their binding is subject to regulation.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingAnimalsCaenorhabditis elegansCell MembraneDishevelled ProteinsDrosophila melanogasterDrosophila ProteinsGene Expression RegulationGuanine Nucleotide Exchange FactorsHumansModels, MolecularPhosphoproteinsProtein BindingProtein Structure, TertiaryRGS ProteinsAdaptor Proteins, Signal TransducingDishevelled ProteinsDrosophila Proteinsdsh protein, DrosophilaGuanine Nucleotide Exchange FactorsPhosphoproteinsPREX1 protein, humanRAPGEF3 protein, humanRGS Proteins

Identifiers

PMID24739740

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.