Evidence map›Paper›PMID 28572448›Full record

ArticleThe EMBO journal2017

Structural and functional dissection of the interplay between lipid and Notch binding by human Notch ligands.

Richard J Suckling, Boguslawa Korona, Pat Whiteman, Chandramouli Chillakuri, Laurie Holt, Penny A Handford, Susan M Lea

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. UtilizingJournal of developmental biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Notch signaling pathway: architecture, disease, and therapeutics.Signal transduction and targeted therapy · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Notch-Jagged signaling complex defined by an interaction mosaic.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Biophysics of Notch Signaling.Annual review of biophysics · 2021
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Richard J SucklingSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Boguslawa KoronaDepartment of Biochemistry, University of Oxford, Oxford, UK.
Pat WhitemanDepartment of Biochemistry, University of Oxford, Oxford, UK.
Chandramouli ChillakuriDepartment of Biochemistry, University of Oxford, Oxford, UK.
Laurie HoltDepartment of Biochemistry, University of Oxford, Oxford, UK.
Penny A HandfordDepartment of Biochemistry, University of Oxford, Oxford, UK penny.handford@bioch.ox.ac.uk susan.lea@path.ox.ac.uk.ORCID 0000-0002-0590-7651
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford, UK penny.handford@bioch.ox.ac.uk susan.lea@path.ox.ac.uk.ORCID 0000-0001-9287-8053
University of Oxford · GB

Funding

Medical Research Council MR/L001187/1Wellcome TrustWellcome Trust 097928Wellcome Trust 100298
6 · The paper itself

Abstract

Recent data have expanded our understanding of Notch signalling by identifying a C2 domain at the N-terminus of Notch ligands, which has both lipid- and receptor-binding properties. We present novel structures of human ligands Jagged2 and Delta-like4 and human Notch2, together with functional assays, which suggest that ligand-mediated coupling of membrane recognition and Notch binding is likely to be critical in establishing the optimal context for Notch signalling. Comparisons between the Jagged and Delta family show a huge diversity in the structures of the loops at the apex of the C2 domain implicated in membrane recognition and Jagged1 missense mutations, which affect these loops and are associated with extrahepatic biliary atresia, lead to a loss of membrane recognition, but do not alter Notch binding. Taken together, these data suggest that C2 domain binding to membranes is an important element in tuning ligand-dependent Notch signalling in different physiological contexts.

Indexed as

Lipid MetabolismCrystallography, X-RayHumansIntracellular Signaling Peptides and ProteinsJagged-2 ProteinMembrane ProteinsModels, MolecularProtein BindingProtein ConformationProtein DomainsReceptor, Notch1Receptor, Notch2delta proteinIntracellular Signaling Peptides and ProteinsJagged-2 ProteinMembrane ProteinsNOTCH1 protein, humanNOTCH2 protein, humanReceptor, Notch1Receptor, Notch2Delta‐likeJaggedlipid‐bindingNotchspecificity

Identifiers

PMID28572448
PMCPMC5538765
OpenAlexW2618346742

What OpenQuestion holds

Textmetadata
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.