Evidence map›Paper›PMID 12975355›Full record

ArticleThe Journal of cell biology2003

Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers.

Maria Traka, Laurence Goutebroze, Natalia Denisenko, Maria Bessa, Artemisia Nifli, Sophia Havaki, Yoichiro Iwakura, Fumihiko Fukamauchi, Kazutada Watanabe, Betty Soliven and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

117 citing papers in PubMed, 239 citations in OpenAlex.

  1. Article
  2. Autism associatedbioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Cytoskeletal scaffolding of NaCurrent opinion in cell biology · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Molecular mechanism of contactin 2 homophilic interaction.Structure (London, England : 1993) · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

57 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

12 authors at 9 institutions in 4 countries.

Maria TrakaDepartment of Basic Science, University of Crete Medical School, Heraklion 71110, Crete, Greece.
Laurence Goutebroze
Natalia Denisenko
Maria Bessa
Artemisia Nifli
Sophia Havaki
Yoichiro Iwakura
Fumihiko Fukamauchi
Kazutada Watanabe
Betty Soliven
Jean-Antoine Girault
Domna Karagogeos
FORTH Institute of Molecular Biology and Biotechnology · GRInserm · FRInstitut du Fer à Moulin · FRNagaoka University of Technology · JPSorbonne Université · FRThe University of Tokyo · JPTokyo Medical and Dental University · JPUniversity of Chicago · USUniversity of Crete · GR

Funding

ION CHANNELS IN DEMYELINATING DISEASESR01NS039346 · NINDS · UNIVERSITY OF CHICAGO · PI SOLIVEN, BETTY C · 2000 to 2003
$1.2M
NINDS NIH HHS R01 NS039346NINDS NIH HHS R01 NS39346-01
6 · The paper itself

Abstract

Myelination results in a highly segregated distribution of axonal membrane proteins at nodes of Ranvier. Here, we show the role in this process of TAG-1, a glycosyl-phosphatidyl-inositol-anchored cell adhesion molecule. In the absence of TAG-1, axonal Caspr2 did not accumulate at juxtaparanodes, and the normal enrichment of shaker-type K+ channels in these regions was severely disrupted, in the central and peripheral nervous systems. In contrast, the localization of protein 4.1B, an axoplasmic partner of Caspr2, was only moderately altered. TAG-1, which is expressed in both neurons and glia, was able to associate in cis with Caspr2 and in trans with itself. Thus, a tripartite intercellular protein complex, comprised of these two proteins, appears critical for axo-glial contacts at juxtaparanodes. This complex is analogous to that described previously at paranodes, suggesting that similar molecules are crucial for different types of axo-glial interactions.

Indexed as

Cytoskeletal ProteinsNeuropeptidesAnimalsBrainCell Adhesion Molecules, NeuronalCell CommunicationCell MembraneContactin 2COS CellsMacromolecular SubstancesMembrane ProteinsMiceMice, KnockoutMicroscopy, ElectronMutationNerve Fibers, MyelinatedCell Adhesion Molecules, NeuronalCNTN2 protein, humanCntn2 protein, mouseCNTNAP2 protein, humanContactin 2Cytoskeletal Proteinserythrocyte membrane band 4.1 proteinerythrocyte membrane protein band 4.1-like 1Macromolecular SubstancesMembrane ProteinsNerve Tissue ProteinsNeuropeptidesPotassium ChannelsShaker Superfamily of Potassium Channels

Identifiers

PMID12975355
PMCPMC2172849
OpenAlexW2156134210

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.