Evidence map›Paper›PMID 19367338›Full record

ArticlePloS one2009

Inhibitory activity of myelin-associated glycoprotein on sensory neurons is largely independent of NgR1 and NgR2 and resides within Ig-Like domains 4 and 5.

Verena Wörter, Rüdiger Schweigreiter, Bernd Kinzel, Matthias Mueller, Carmen Barske, Günther Böck, Stefan Frentzel, Christine E Bandtlow

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Complement protein C1q modulates neurite outgrowth in vitro and spinal cord axon regeneration in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  9. Article
  10. Review
  11. Nogo receptor homolog NgR2 expressed in sensory DRG neurons controls epidermal innervation by interaction with Versican.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. High affinity sialoside ligands of myelin associated glycoprotein.Bioorganic & medicinal chemistry letters · 2011
    Article
  18. Article
  19. Article
  20. Guidance molecules in axon regeneration.Cold Spring Harbor perspectives in biology · 2010
    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

8 authors at 2 institutions in 2 countries.

Verena WörterInnsbruck Medical University, Biocenter, Division of Neurobiochemistry, Innsbruck, Austria.
Rüdiger Schweigreiter
Bernd Kinzel
Matthias Mueller
Carmen Barske
Günther Böck
Stefan Frentzel
Christine E Bandtlow
Innsbruck Medical University · ATNovartis (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myelin-associated glycoprotein (MAG) is a sialic acid binding Ig-like lectin (Siglec) which has been characterized as potent myelin-derived inhibitor of neurite outgrowth. Two members of the Nogo-receptor (NgR) family, NgR1 and NgR2, have been identified as neuronal binding proteins of MAG. In addition, gangliosides have been proposed to bind to and confer the inhibitory activity of MAG on neurons. In this study, we investigated the individual contribution of NgRs and gangliosides to MAG-mediated inhibition of sensory neurons derived from dorsal root ganglia (DRG) of ngr1, ngr2 or ngr1/ngr2 deletion mutants. We found no disinhibition of neurite growth in the absence of either NgR1 or NgR2. Sensory neurons deficient for both NgR proteins displayed only a moderate reduction of MAG-mediated inhibition of neurite growth. If treated with Vibrio cholerae neuraminidase (VCN), inhibition by MAG is further attenuated but still not annulled. Thus, disrupting all known protein and ganglioside receptors for MAG in sensory neurons does not fully abolish its inhibitory activity pointing to the existence of as yet unidentified receptors for MAG. Moreover, by employing a variety of protein mutants, we identified the Ig-like domains 4 or 5 of MAG as necessary and sufficient for growth arrest, whereas abolishing MAG's ability to bind to sialic acid did not interfere with its inhibitory activity. These findings provide new insights into the inhibitory function of MAG and suggest similarities but also major differences in MAG inhibition between sensory and central nervous system (CNS) neurons.

Indexed as

Neural InhibitionAnimalsBinding SitesGangliosidesHumansLectinsMiceMice, KnockoutMyelin-Associated GlycoproteinMyelin-Oligodendrocyte GlycoproteinMyelin ProteinsN-Acetylneuraminic AcidNeuraminidaseNeuritesNogo ProteinsProtein Structure, TertiaryGangliosidesLectinsMOG protein, humanMog protein, mouseMyelin-Associated GlycoproteinMyelin-Oligodendrocyte GlycoproteinMyelin ProteinsN-Acetylneuraminic AcidNeuraminidaseNogo ProteinsRTN4 protein, humanRtn4 protein, mouseSialic Acid Binding Immunoglobulin-like Lectins

Identifiers

PMID19367338
PMCPMC2666269
OpenAlexW1984698452

What OpenQuestion holds

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LicenceCC BY
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.