Evidence map›Paper›PMID 18093521›Full record

ArticleNeuron2007

Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion.

Igor P Fabrichny, Philippe Leone, Gerlind Sulzenbacher, Davide Comoletti, Meghan T Miller, Palmer Taylor, Yves Bourne, Pascale Marchot

Open access · bronzeAbstract readComment
In one paragraph

Article in Neuron, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

88 citing papers in PubMed, 146 citations in OpenAlex.

  1. Review
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. An Autism-Associated Mutation Impairs Neuroligin-4 Glycosylation and Enhances Excitatory Synaptic Transmission in Human Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  17. Review
  18. Article
  19. Article
  20. Article

28 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Igor P FabrichnyBiochimie des Interactions Moléculaires et Cellulaires, CNRS FRE-2738, Institut Fédératif de Recherche Jean Roche, Université de la Méditerranée, Faculté de Médecine Secteur Nord, F-13916 Marseille Cedex 20, France.
Philippe Leone
Gerlind Sulzenbacher
Davide Comoletti
Meghan T Miller
Palmer Taylor
Yves Bourne
Pascale Marchot
Aix-Marseille Université · FRRoche (Switzerland) · CH

Funding

Yeast Genetics and Stress Response Genes-BiomedicalP42ES010337 · NIEHS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TUKEY, ROBERT H · 2000 to 2022
$69.8M
GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
KINETICS OF DRUG MACROMOLECULE COMPLEX FORMATIONR37GM018360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 1999 to 2008
$5.7M
KINETICS OF DRUG-MACROMOLECULE COMPLEX FORMATIONR01GM018360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 1985 to 2013
$2.8M
NIEHS NIH HHS P42 ES010337NIEHS NIH HHS UO-1 ES 10337NIGMS NIH HHS GM07752NIGMS NIH HHS R01 GM018360NIGMS NIH HHS R37 GM018360NIGMS NIH HHS R37-GM 18360NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

The neuroligins are postsynaptic cell adhesion proteins whose associations with presynaptic neurexins participate in synaptogenesis. Mutations in the neuroligin and neurexin genes appear to be associated with autism and mental retardation. The crystal structure of a neuroligin reveals features not found in its catalytically active relatives, such as the fully hydrophobic interface forming the functional neuroligin dimer; the conformations of surface loops surrounding the vestigial active center; the location of determinants that are critical for folding and processing; and the absence of a macromolecular dipole and presence of an electronegative, hydrophilic surface for neurexin binding. The structure of a beta-neurexin-neuroligin complex reveals the precise orientation of the bound neurexin and, despite a limited resolution, provides substantial information on the Ca2+-dependent interactions network involved in trans-synaptic neurexin-neuroligin association. These structures exemplify how an alpha/beta-hydrolase fold varies in surface topography to confer adhesion properties and provide templates for analyzing abnormal processing or recognition events associated with autism.

Indexed as

Protein FoldingAnimalsCalciumCarotenoidsCell AdhesionCell Line, TransformedHumansMembrane ProteinsModels, MolecularMolecular Sequence DataMutationProtein BindingProtein Structure, TertiaryRatsRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationCalciumCarotenoidsMembrane ProteinsnorbixinRecombinant Proteins

Identifiers

PMID18093521
PMCPMC2703725
OpenAlexW2129700237

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.