ArticleLipids2008
Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1.
Article in Lipids, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed.
- ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes.Cell reports · 2021Article
- Nutrient-induced intestinal adaption and its effect in obesity.Physiology & behavior · 2014Review
- Structural insights into the inhibition of Wnt signaling by cancer antigen 5T4/Wnt-activated inhibitory factor 1.Structure (London, England : 1993) · 2014Article
- Prediction of structure of human WNT-CRD (FZD) complex for computational drug repurposing.PloS one · 2013Article
- The Drosophila WIF1 homolog Shifted maintains glypican-independent Hedgehog signaling and interacts with the Hedgehog co-receptors Ihog and Boi.Development (Cambridge, England) · 2013Article
- Wnt proteins.Cold Spring Harbor perspectives in biology · 2012Review
- The role of glypicans in Wnt inhibitory factor-1 activity and the structural basis of Wif1's effects on Wnt and Hedgehog signaling.PLoS genetics · 2012Article
- Modular mechanism of Wnt signaling inhibition by Wnt inhibitory factor 1.Nature structural & molecular biology · 2011Article
- microRNAs and Corresponding Targets Involved in Metastasis of Colorectal Cancer in PreclinicalCancer genomics & proteomicsReview
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Palmitoylated Wnt proteins comprise a conserved family of secreted signaling molecules associated with variety of human cancers. WIF domain of the human WIF (Wnt inhibitory factor)-1 is sufficient for Wnt binding and signaling inhibition. Detailed interactions between Wnt and WIF-1 are not known. Computational docking was employed to identify a possible fatty acid binding site in the WIF domain. A putative binding site was identified inside the domain. WIF domain exhibited the highest affinity for C16:0-C18:0 (-22 kJ/mol free energy of binding) fatty acids. The results suggest a role of the WIF domain as a palmitoyl binding domain required for WIF-1 binding to palmitoylated Wnt and signaling inhibition.
Indexed as
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18256869What OpenQuestion holds
Registered trials
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.