Evidence map›Paper›PMID 18456828›Full record

ArticleBiophysical journal2008

Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3.

Aviv Paz, Tzviya Zeev-Ben-Mordehai, Martin Lundqvist, Eilon Sherman, Efstratios Mylonas, Lev Weiner, Gilad Haran, Dmitri I Svergun, Frans A A Mulder, Joel L Sussman and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
7.9field-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

23 citing papers in PubMed, 53 citations in OpenAlex.

  1. Semi-synthesis of the C-terminal region ofRSC chemical biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Accurate model of liquid-liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Bacterial functional amyloids: Order from disorder.Biochimica et biophysica acta. Proteins and proteomics · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Context-dependent resistance to proteolysis of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2011
    Review
  19. Article
  20. Article
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

11 authors at 4 institutions in 4 countries.

Aviv PazDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Tzviya Zeev-Ben-Mordehai
Martin Lundqvist
Eilon Sherman
Efstratios Mylonas
Lev Weiner
Gilad Haran
Dmitri I Svergun
Frans A A Mulder
Joel L Sussman
Israel Silman
Weizmann Institute of Science · ILUniversity of Groningen · NLA.V. Shubnikov Institute of Crystallography · RUEuropean Molecular Biology Laboratory · DE

Funding

Autism Speaks AS1324
6 · The paper itself

Abstract

Cholinesterase-like adhesion molecules (CLAMs) are a family of neuronal cell adhesion molecules with important roles in synaptogenesis, and in maintaining structural and functional integrity of the nervous system. Our earlier study on the cytoplasmic domain of one of these CLAMs, the Drosophila protein, gliotactin, showed that it is intrinsically unstructured in vitro. Bioinformatic analysis suggested that the cytoplasmic domains of other CLAMs are also intrinsically unstructured, even though they bear no sequence homology to each other or to any known protein. In this study, we overexpress and purify the cytoplasmic domain of human neuroligin 3, notwithstanding its high sensitivity to the Escherichia coli endogenous proteases that cause its rapid degradation. Using bioinformatic analysis, sensitivity to proteases, size exclusion chromatography, fluorescence correlation spectroscopy, analytical ultracentrifugation, small angle x-ray scattering, circular dichroism, electron spin resonance, and nuclear magnetic resonance, we show that the cytoplasmic domain of human neuroligin 3 is intrinsically unstructured. However, several of these techniques indicate that it is not fully extended, but becomes significantly more extended under denaturing conditions.

Indexed as

Models, ChemicalModels, MolecularBiophysicsCell Adhesion MoleculesCell Adhesion Molecules, NeuronalComputer SimulationCytoplasmHumansMembrane ProteinsNerve Tissue ProteinsProtein ConformationProtein Structure, TertiaryCell Adhesion MoleculesCell Adhesion Molecules, NeuronalMembrane ProteinsNerve Tissue Proteinsneuroligin 3

Identifiers

PMID18456828
PMCPMC2483779
OpenAlexW2155685362

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.