Evidence map›Paper›PMID 9927700›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses.

J Y Song, K Ichtchenko, T C Südhof, N Brose

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 336 papers.

0numbers the graph read from it
0cells of the map it votes in
336citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

336 citing papers in PubMed, 690 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. bioRxiv : the preprint server for biology · 2026
    Article
  8. Differences in blood levels of neuroligin-derived peptides in a cohort for early detection of Alzheimer's disease.The journals of gerontology. Series A, Biological sciences and medical sciences · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

276 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

4 authors at 3 institutions in 2 countries.

J Y SongMax-Planck-Institut für Experimentelle Medizin, Abteilung Molekulare Neurobiologie, Hermann-Rein-Strasse 3, D-37075 Göttingen, Germany.
K Ichtchenko
T C Südhof
N Brose
Max Planck Institute of Experimental Medicine · DESouthwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

NIMH NIH HHS R01-MH50824
6 · The paper itself

Abstract

At the synapse, presynaptic membranes specialized for vesicular traffic are linked to postsynaptic membranes specialized for signal transduction. The mechanisms that connect pre- and postsynaptic membranes into synaptic junctions are unknown. Neuroligins and beta-neurexins are neuronal cell-surface proteins that bind to each other and form asymmetric intercellular junctions. To test whether the neuroligin/beta-neurexin junction is related to synapses, we generated and characterized monoclonal antibodies to neuroligin 1. With these antibodies, we show that neuroligin 1 is synaptic. The neuronal localization, subcellular distribution, and developmental expression of neuroligin 1 are similar to those of the postsynaptic marker proteins PSD-95 and NMDA-R1 receptor. Quantitative immunogold electron microscopy demonstrated that neuroligin 1 is clustered in synaptic clefts and postsynaptic densities. Double immunofluorescence labeling revealed that neuroligin 1 colocalizes with glutamatergic but not gamma-aminobutyric acid (GABA)ergic synapses. Thus neuroligin 1 is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors, channels, and signal-transduction molecules to synaptic sites of cell adhesion. In addition, the neuroligin/beta-neurexin junction may be involved in the specification of excitatory synapses.

Indexed as

Gene Expression Regulation, DevelopmentalAgingAnimalsBrainCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCerebellumCOS CellsDisks Large Homolog 4 ProteinEmbryonic and Fetal DevelopmentGuanylate KinasesHippocampusIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMice, Inbred C57BLCell Adhesion MoleculesCell Adhesion Molecules, NeuronalDisks Large Homolog 4 ProteinDlg4 protein, mouseDlg4 protein, ratGuanylate KinasesIntracellular Signaling Peptides and ProteinsMembrane ProteinsNerve Tissue Proteinsneuroligin 1postsynaptic density proteinsReceptors, N-Methyl-D-AspartateSynaptophysin

Identifiers

PMID9927700
PMCPMC15357
OpenAlexW2100414555

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.