Evidence map›Paper›PMID 28533339›Full record

ArticleThe Journal of biological chemistry2017

Structure-based prediction of Wnt binding affinities for Frizzled-type cysteine-rich domains.

Mark Agostino, Sebastian Öther-Gee Pohl, Arun Dharmarajan

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. MultilevelCurrent research in structural biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Unleashing Wnts: Wnt Ligands Fuel Cancer Spread.Journal of cancer biology · 2025
    Article
  10. Frizzled receptors: gatekeepers of Wnt signaling in development and disease.Frontiers in cell and developmental biology · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. The role of WNT10B in physiology and disease: A 10-year update.Frontiers in cell and developmental biology · 2023
    Review
  17. Article
  18. Sfrp4 and the Biology of Cortical Bone.Current osteoporosis reports · 2022
    Review
  19. Review
  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

3 authors.

Mark AgostinoFrom the Stem Cell and Cancer Biology Laboratory, School of Biomedical Sciences and Curtin Health Innovation Research Institute and Mark.Agostino@curtin.edu.au.ORCID 0000-0002-1799-0392
Sebastian Öther-Gee PohlFrom the Stem Cell and Cancer Biology Laboratory, School of Biomedical Sciences and Curtin Health Innovation Research Institute and.
Arun DharmarajanFrom the Stem Cell and Cancer Biology Laboratory, School of Biomedical Sciences and Curtin Health Innovation Research Institute and.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Wnt signaling pathways are of significant interest in development and oncogenesis. The first step in these pathways typically involves the binding of a Wnt protein to the cysteine-rich domain (CRD) of a Frizzled receptor. Wnt-Frizzled interactions can be antagonized by secreted Frizzled-related proteins (SFRPs), which also contain a Frizzled-like CRD. The large number of Wnts, Frizzleds, and SFRPs, as well as the hydrophobic nature of Wnt, poses challenges to laboratory-based investigations of interactions involving Wnt. Here, utilizing structural knowledge of a representative Wnt-Frizzled CRD interaction, as well as experimentally determined binding affinities for a selection of Wnt-Frizzled CRD interactions, we generated homology models of Wnt-Frizzled CRD interactions and developed a quantitative structure-activity relationship for predicting their binding affinities. The derived model incorporates a small selection of terms derived from scoring functions used in protein-protein docking, as well as an energetic term considering the contribution made by the lipid of Wnt to the Wnt-Frizzled binding affinity. Validation with an external test set suggests that the model can accurately predict binding affinity for 75% of cases and that the error associated with the predictions is comparable with the experimental error. The model was applied to predict the binding affinities of the full range of mouse and human Wnt-Frizzled and Wnt-SFRP interactions, indicating trends in Wnt binding affinity for Frizzled and SFRP CRDs. The comprehensive predictions made in this study provide the basis for laboratory-based studies of previously unexplored Wnt-Frizzled and Wnt-SFRP interactions, which, in turn, may reveal further Wnt signaling pathways.

Indexed as

Frizzled ReceptorsMolecular Docking SimulationWnt ProteinsAnimalsHumansProtein BindingProtein DomainsWnt Signaling PathwayFrizzled ReceptorsWnt Proteinscysteine-rich domainFrizzled receptorhomology modelinglipid-protein interactionprotein-protein interactionstructural biologystructure-activity relationshipWnt signaling

Identifiers

PMID28533339
PMCPMC5500790

What OpenQuestion holds

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Registered trials

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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.