Evidence map›Paper›PMID 9118959›Full record

ArticleThe EMBO journal1997

Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions.

E Peles, M Nativ, M Lustig, M Grumet, J Schilling, R Martinez, G D Plowman, J Schlessinger

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed
8.6field-weighted citation impact, top 1% 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

175 citing papers in PubMed, 406 citations in OpenAlex.

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  6. Targeting the muscarinic M1 receptor with a selective, brain-penetrant antagonist to promote remyelination in multiple sclerosis.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  10. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  11. Article
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  15. Finding New Ways How to Control BACE1.The Journal of membrane biology · 2022
    Article
  16. Paranodal Axoglial Junctions, an Essential Component in Axonal Homeostasis.Frontiers in cell and developmental biology · 2022
    Review
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  19. 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
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  20. Mechanisms of node of Ranvier assembly.Nature reviews. Neuroscience · 2021
    Review

115 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

8 authors at 1 institution in 1 country.

E PelesSugen, Inc., Redwood City, CA 94063, USA.
M Nativ
M Lustig
M Grumet
J Schilling
R Martinez
G D Plowman
J Schlessinger
Maxygen (United States) · US

Funding

MOLECULAR MECHANISMS OF NEURON-GLIA ADHESIONR01NS021629 · NINDS · ROCKEFELLER UNIVERSITY · PI GRUMET, MARTIN H · 1985 to 1996
–
NINDS NIH HHS NS21629
6 · The paper itself

Abstract

Receptor protein tyrosine phosphatase beta (RPTPbeta) expressed on the surface of glial cells binds to the glycosylphosphatidylinositol (GPI)-anchored recognition molecule contactin on neuronal cells leading to neurite outgrowth. We describe the cloning of a novel contactin-associated transmembrane receptor (p190/Caspr) containing a mosaic of domains implicated in protein-protein interactions. The extracellular domain of Caspr contains a neurophilin/coagulation factor homology domain, a region related to fibrinogen beta/gamma, epidermal growth factor-like repeats, neurexin motifs as well as unique PGY repeats found in a molluscan adhesive protein. The cytoplasmic domain of Caspr contains a proline-rich sequence capable of binding to a subclass of SH3 domains of signaling molecules. Caspr and contactin exist as a complex in rat brain and are bound to each other by means of lateral (cis) interactions in the plasma membrane. We propose that Caspr may function as a signaling component of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons. The binding of RPTPbeta to the contactin-Caspr complex could provide a mechanism for cell-cell communication between glial cells and neurons during development.

Indexed as

Cell Adhesion Molecules, NeuronalAmino Acid SequenceAnimalsBlotting, WesternCell MembraneCloning, MolecularContactinsGene ExpressionHumansImmunohistochemistryMolecular Sequence DataNerve Tissue ProteinsNeuronsProtein BindingRatsReceptors, Cell SurfaceCell Adhesion Molecules, NeuronalCNTNAP1 protein, humanCntnap1 protein, ratContactinsNerve Tissue ProteinsReceptors, Cell SurfaceRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID9118959
PMCPMC1169698
OpenAlexW2098584548

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.