Evidence map›Paper›PMID 25482632›Full record

ReviewCell adhesion & migration2014

The role of proteases in regulating Eph/ephrin signaling.

Lakmali Atapattu, Martin Lackmann, Peter W Janes

Open access · goldAbstract readReview
In one paragraph

Review in Cell adhesion & migration, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. A Valuable Target for Therapy: The Metalloproteinase ADAM10.Current protein & peptide science · 2025
    Review
  4. Article
  5. Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024
    Review
  6. Nogo-A is secreted in extracellular vesicles, occurs in blood and can influence vascular permeability.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Cancers · 2021
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  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 at 1 institution in 1 country.

Lakmali Atapattua Department of Biochemistry and Molecular Biology ; Monash University , Victoria ; Australia.
Martin Lackmann
Peter W Janes
Monash University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteases regulate a myriad of cell functions, both in normal and disease states. In addition to protein turnover, they regulate a range of signaling processes, including those mediated by Eph receptors and their ephrin ligands. A variety of proteases is reported to directly cleave Ephs and/or ephrins under different conditions, to promote receptor and/or ligand shedding, and regulate receptor/ligand internalisation and signaling. They also cleave other adhesion proteins in response to Eph-ephrin interactions, to indirectly facilitate Eph-mediated functions. Proteases thus contribute to Eph/ephrin mediated changes in cell-cell and cell-matrix interactions, in cell morphology and in cell migration and invasion, in a manner which appears to be tightly regulated by, and co-ordinated with, Eph signaling. This review summarizes the current literature describing the function and regulation of protease activities during Eph/ephrin-mediated cell signaling.

Indexed as

Cell MovementSignal TransductionAnimalsCell AdhesionCell CommunicationEphrinsHumansLigandsMicePeptide HydrolasesProtein BindingReceptors, Eph FamilyEphrinsLigandsPeptide HydrolasesReceptors, Eph FamilyAD, Alzheimer's disease; ADAM, a disintegrin and metalloprotease; APP, Amyloid precursor protein; Arf1, ADP rybosylation factor 1; BACE, β-site APP cleaving enzyme; CAM, cell adhesion molecules; CTF, cytoplasmic fragment; CNC, cranial neural crest; ECM,ADAMEph receptor tyrosine kinaseephrin signalingMMPproteaseγ-secretase

Identifiers

PMID25482632
PMCPMC4594553
OpenAlexW1969398711

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.