Evidence map›Paper›PMID 17967169›Full record

ArticleBMC neuroscience2007

The adhesion molecule Necl-3/SynCAM-2 localizes to myelinated axons, binds to oligodendrocytes and promotes cell adhesion.

François Pellissier, Alan Gerber, Christoph Bauer, Marc Ballivet, Vincent Ossipow

Open access · goldAbstract read
In one paragraph

Article in BMC neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

21 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Differential Contribution of Cadm1-Cadm3 Cell Adhesion Molecules to Peripheral Myelinated Axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Genetic deletion of Cadm4 results in myelin abnormalities resembling Charcot-Marie-Tooth neuropathy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  17. Article
  18. Article
  19. Signals to promote myelin formation and repair.Nature reviews. Neurology · 2010
    Review
  20. Disruption of Nectin-like 1 cell adhesion molecule leads to delayed axonal myelination in the CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    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

5 authors at 1 institution in 1 country.

François PellissierDepartment of Biochemistry, University of Geneva, 30 Quai Ernest Ansermet, Sciences II, 1211 Geneva 4, Switzerland. francois.pellissier@biochem.unige.ch
Alan Gerber
Christoph Bauer
Marc Ballivet
Vincent Ossipow
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCell adhesion molecules are plasma membrane proteins specialized in cell-cell recognition and adhesion. Two related adhesion molecules, Necl-1 and Necl-2/SynCAM, were recently described and shown to fulfill important functions in the central nervous system. The purpose of the work was to investigate the distribution, and the properties of Necl-3/SynCAM-2, a previously uncharacterized member of the Necl family with which it shares a conserved modular organization and extensive sequence homology.

resultsWe show that Necl-3/SynCAM-2 is a plasma membrane protein that accumulates in several tissues, including those of the central and peripheral nervous system. There, Necl-3/SynCAM-2 is expressed in ependymal cells and in myelinated axons, and sits at the interface between the axon shaft and the myelin sheath. Several independent assays demonstrate that Necl-3/SynCAM-2 functionally and selectively interacts with oligodendrocytes. We finally prove that Necl-3/SynCAM-2 is a bona fide adhesion molecule that engages in homo- and heterophilic interactions with the other Necl family members, leading to cell aggregation.

conclusionCollectively, our manuscripts and the works on Necl-1 and SynCAM/Necl-2 reveal a complex set of interactions engaged in by the Necl proteins in the nervous system. Our work also support the notion that the family of Necl proteins fulfils key adhesion and recognition functions in the nervous system, in particular between different cell types.

Indexed as

AnimalsBrainCell AdhesionCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell LineDrosophila melanogasterEpendymaHeLa CellsHumansImmunoglobulinsMembrane ProteinsMicroscopy, ImmunoelectronMyelin SheathNerve Fibers, MyelinatedOligodendrogliaCadm1 protein, ratCadm2 protein, ratCell Adhesion MoleculesCell Adhesion Molecules, NeuronalImmunoglobulinsMembrane ProteinsProtein IsoformsTumor Suppressor Proteins

Identifiers

PMID17967169
PMCPMC2176061
OpenAlexW2019367102

What OpenQuestion holds

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LicenceCC BY
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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.