Evidence map›Paper›PMID 24239355›Full record

ArticleCell reports2013

Structural analysis uncovers lipid-binding properties of Notch ligands.

Chandramouli R Chillakuri, Devon Sheppard, Ma Xenia G Ilagan, Laurie R Holt, Felicity Abbott, Shaoyan Liang, Raphael Kopan, Penny A Handford, Susan M Lea

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. UtilizingJournal of developmental biology · 2025
    Review
  4. Article
  5. Article
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  7. Article
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  9. Review
  10. Mutations inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Notch-Jagged signaling complex defined by an interaction mosaic.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Biophysics of Notch Signaling.Annual review of biophysics · 2021
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Chandramouli R ChillakuriDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Devon Sheppard
Ma Xenia G Ilagan
Laurie R Holt
Felicity Abbott
Shaoyan Liang
Raphael Kopan
Penny A Handford
Susan M Lea
University of Oxford · GBWashington University in St. Louis · US

Funding

Wellcome Trust 087928Wellcome Trust 100298
6 · The paper itself

Abstract

The Notch pathway is a core cell-cell signaling system in metazoan organisms with key roles in cell-fate determination, stem cell maintenance, immune system activation, and angiogenesis. Signals are initiated by extracellular interactions of the Notch receptor with Delta/Serrate/Lag-2 (DSL) ligands, whose structure is highly conserved throughout evolution. To date, no structure or activity has been associated with the extreme N termini of the ligands, even though numerous mutations in this region of Jagged-1 ligand lead to human disease. Here, we demonstrate that the N terminus of human Jagged-1 is a C2 phospholipid recognition domain that binds phospholipid bilayers in a calcium-dependent fashion. Furthermore, we show that this activity is shared by a member of the other class of Notch ligands, human Delta-like-1, and the evolutionary distant Drosophila Serrate. Targeted mutagenesis of Jagged-1 C2 domain residues implicated in calcium-dependent phospholipid binding leaves Notch interactions intact but can reduce Notch activation. These results reveal an important and previously unsuspected role for phospholipid recognition in control of this key signaling system.

Indexed as

Amino Acid SequenceCalciumCalcium-Binding ProteinsCell DifferentiationCell LineCrystallography, X-RayDrosophila ProteinsEnzyme ActivationFatty Acid-Binding ProteinsHEK293 CellsHumansIntercellular Signaling Peptides and ProteinsJagged-1 ProteinMembrane ProteinsMolecular Sequence DataPhospholipidsCalciumCalcium-Binding ProteinsDLK1 protein, humanDrosophila ProteinsFatty Acid-Binding ProteinsIntercellular Signaling Peptides and ProteinsJAG1 protein, humanJagged-1 ProteinMembrane ProteinsPhospholipidsReceptors, NotchSer protein, DrosophilaSerrate-Jagged Proteins

Identifiers

PMID24239355
PMCPMC3888931
OpenAlexW2139428600

What OpenQuestion holds

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LicenceCC BY
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.