ArticleInternational journal of molecular sciences2019
Wnt Binding Affinity Prediction for Putative Frizzled-Type Cysteine-Rich Domains.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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.
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Who cites it
13 citing papers in PubMed.
- MultilevelCurrent research in structural biology · 2026Article
- Refolding Protocol of the Cysteine-Rich Domain of Frizzled8 from Inclusion Bodies.International journal of molecular sciences · 2026Article
- Frizzled receptors: gatekeepers of Wnt signaling in development and disease.Frontiers in cell and developmental biology · 2025Review
- Article
- Compound heterozygous WNT10A missense variations exacerbated the tooth agenesis caused by hypohidrotic ectodermal dysplasia.BMC oral health · 2024Article
- Article
- Functional role of the Frizzled linker domain in the Wnt signaling pathway.Communications biology · 2022Article
- Novel Biomolecules in the Pathogenesis of Gestational Diabetes Mellitus 2.0.International journal of molecular sciences · 2022Review
- Review
- Quantitative Profiling of WNT-3A Binding to All Human Frizzled Paralogues in HEK293 Cells by NanoBiT/BRET Assessments.ACS pharmacology & translational science · 2021Article
- Secreted Frizzled Related Proteins in Cardiovascular and Metabolic Diseases.Frontiers in endocrinology · 2021Review
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Comment on: "Wnt Binding Affinity Prediction for Putative Frizzled-Type Cysteine-Rich Domains".International journal of molecular sciences · 2019Article
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2 authors.
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Abstract
Several proteins other than the frizzled receptors (Fzd) and the secreted Frizzled-related proteins (sFRP) contain Fzd-type cysteine-rich domains (CRD). We have termed these domains "putative Fzd-type CRDs", as the relevance of Wnt signalling in the majority of these is unknown; the RORs, an exception to this, are well known for mediating non-canonical Wnt signalling. In this study, we have predicted the likely binding affinity of all Wnts for all putative Fzd-type CRDs. We applied both our previously determined Wnt‒Fzd CRD binding affinity prediction model, as well as a newly devised model wherein the lipid term was forced to contribute favourably to the predicted binding energy. The results obtained from our new model indicate that certain putative Fzd CRDs are much more likely to bind Wnts, in some cases exhibiting selectivity for specific Wnts. The results of this study inform the investigation of Wnt signalling modulation beyond Fzds and sFRPs.
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