Evidence map›Paper›PMID 17562316›Full record

ArticleStructure (London, England : 1993)2007

Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering.

Davide Comoletti, Alexander Grishaev, Andrew E Whitten, Igor Tsigelny, Palmer Taylor, Jill Trewhella

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
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  12. Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Dimerization of postsynaptic neuroligin drives synaptic assembly via transsynaptic clustering of neurexin.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Review
  20. Neurexins and neuroligins: synapses look out of the nervous system.Cellular and molecular life sciences : CMLS · 2011
    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

6 authors at 3 institutions in 2 countries.

Davide ComolettiDepartment of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California-San Diego, La Jolla, CA 92093, USA. dcomolet@ucsd.edu
Alexander Grishaev
Andrew E Whitten
Igor Tsigelny
Palmer Taylor
Jill Trewhella
University of Montana · USUniversity of Sydney · AUNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Yeast Genetics and Stress Response Genes-BiomedicalP42ES010337 · NIEHS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TUKEY, ROBERT H · 2000 to 2022
$69.8M
KINETICS OF DRUG MACROMOLECULE COMPLEX FORMATIONR37GM018360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, PALMER WILLIAM · 1999 to 2008
$5.7M
Intramural NIH HHSNIEHS NIH HHS P42 ES010337NIEHS NIH HHS P42 ES 10337NIGMS NIH HHS R37 GM018360NIGMS NIH HHS R37 GM 18360
6 · The paper itself

Abstract

Neuroligins are postsynaptic cell-adhesion proteins that associate with their presynaptic partners, the neurexins. Using small-angle X-ray scattering, we determined the shapes of the extracellular region of several neuroligin isoforms in solution. We conclude that the neuroligins dimerize via the characteristic four-helix bundle observed in cholinesterases, and that the connecting sequence between the globular lobes of the dimer and the cell membrane is elongated, projecting away from the dimer interface. X-ray scattering and neutron contrast variation data show that two neurexin monomers, separated by 107 A, bind at symmetric locations on opposite sides of the long axis of the neuroligin dimer. Using these data, we developed structural models that delineate the spatial arrangements of different neuroligin domains and their partnering molecules. As mutations of neurexin and neuroligin genes appear to be linked to autism, these models provide a structural framework for understanding altered recognition by these proteins in neurodevelopmental disorders.

Indexed as

Neutron DiffractionScattering, Small AngleX-Ray DiffractionAmino Acid SequenceAnimalsCell Adhesion Molecules, NeuronalDimerizationMembrane ProteinsModels, ChemicalModels, MolecularMolecular Sequence DataMutationNerve Tissue ProteinsProtein IsoformsProtein Structure, SecondaryProtein Structure, TertiaryCell Adhesion Molecules, NeuronalMembrane ProteinsNerve Tissue Proteinsneuroligin 1Protein IsoformsRecombinant Proteins

Identifiers

PMID17562316
PMCPMC2677967
OpenAlexW1984795378

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.