Evidence map›Paper›PMID 8641271›Full record

ArticleThe EMBO journal1996

Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site.

C Rader, B Kunz, R Lierheimer, R J Giger, P Berger, P Tittmann, H Gross, P Sonderegger

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 74 citations in OpenAlex.

  1. Molecular mechanism of contactin 2 homophilic interaction.Structure (London, England : 1993) · 2024
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  8. TAG1 regulates the endocytic trafficking and signaling of the semaphorin3A receptor complex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
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  10. Lewis(x) and alpha2,3-sialyl glycans and their receptors TAG-1, Contactin, and L1 mediate CD24-dependent neurite outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  11. Structural requirement of TAG-1 for retinal ganglion cell axons and myelin in the mouse optic nerve.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
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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 1 institution in 1 country.

C RaderInstitute of Biochemistry, University of Zurich, Switzerland.
B Kunz
R Lierheimer
R J Giger
P Berger
P Tittmann
H Gross
P Sonderegger
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neuronal cell adhesion molecule axonin-1 is composed of six immunoglobulin and four fibronectin type III domains. Axonin-1 promotes neurite outgrowth, when presented as a substratum for neurons in vitro, via a neuronal receptor that has been identified as the neuron-glia cell adhesion molecule, NgCAM, based on the blocking effect of polyclonal antibodies directed to NgCAM. Here we report the identification of axonin-1 domains involved in NgCAM binding. NgCAM-conjugated microspheres were tested for binding to COS cells expressing domain deletion mutants of axonin-1. In addition, monoclonal antibodies directed to axonin-1 were assessed for their ability to block the axonin-1-NgCAM interaction, and their epitopes were mapped using the domain deletion mutants. The results suggest that the four amino-terminal immunoglobulin domains of axonin-1 form a domain conglomerate which is necessary and sufficient for NgCAM binding. Surprisingly, NgCAM binding to membrane-bound axonin-1 was increased strongly by deletion of the fifth or sixth immunoglobulin domains of axonin-1. Based on these results and on negative staining electron microscopy, we propose a horseshoe-shaped domain arrangement of axonin-1 that obscures the NgCAM binding site. Neurite outgrowth studies with truncated forms of axonin-1 show that axonin-1 is a neurite outgrowth-promoting substratum in the absence of the NgCAM binding site.

Indexed as

AnimalsBase SequenceBinding SitesCell Adhesion Molecules, NeuronalCell Adhesion Molecules, Neuron-GliaCell LineChick EmbryoContactin 2Microscopy, ElectronMolecular Sequence DataNeuritesOligodeoxyribonucleotidesProtein BindingProtein FoldingCell Adhesion Molecules, NeuronalCell Adhesion Molecules, Neuron-GliaContactin 2Oligodeoxyribonucleotides

Identifiers

PMID8641271
PMCPMC450127
OpenAlexW2297808440

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.