Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The crystal structure of full-length Sizzled from Xenopus laevis yields insights into Wnt-antagonistic function of secreted Frizzled-related proteins.

The Journal of biological chemistry - 29 Sept 2017

Bu Qixin, Li Zhiqiang, Zhang Junying, Xu Fei, Liu Jianmei, Liu Heli

Abstract excerpt

The Wnt-signaling pathway is crucial to cell proliferation, differentiation, and migration. The secreted Frizzled-related proteins (sFRPs) represent the largest family of secreted Wnt inhibitors. However, their function in antagonizing Wnt signaling has remained somewhat controversial. Here, we report the crystal structure of Sizzled from Xenopus laevis, the first full-length structure of an sFRP. Tethered by an...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Databases, Protein
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptide Fragments

Share to Protein Interaction Domains and Motifs

Share to Wnt Proteins

Share to Wnt Signaling Pathway

Share to Xenopus laevis

Share to Xenopus Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 28808056
DOI: 10.1074/jbc.M117.791756
PMCID: PMC5625038

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The crystal structure of full-length Sizzled from Xenopus laevis yields insights into Wnt-antagonistic function of secreted Frizzled-related proteins.PMID 28808056Read ↗

Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains.Semantic proximity Read ↗

The Netrin-related domain of Sfrp1 interacts with Wnt ligands and antagonizes their activity in the anterior neural plate.Semantic proximity Read ↗

Rational design of DKK3 structure-based small peptides as antagonists of Wnt signaling pathway and in silico evaluation of their efficiencySemantic proximity Read ↗

The role of the cysteine-rich domain of Frizzled in Wingless-Armadillo signaling.Semantic proximity Read ↗

Protease associated domain of RNF43 is not necessary for the suppression of Wnt/β-catenin signaling in human cells.Semantic proximity Read ↗

Evidence that the cysteine-rich domain of Drosophila Frizzled family receptors is dispensable for transducing Wingless.Semantic proximity Read ↗

Dishevelled promotes Wnt receptor degradation through recruitment of ZNRF3/RNF43 E3 ubiquitin ligases.Semantic proximity Read ↗

The structural basis of R-spondin recognition by LGR5 and RNF43.Semantic proximity Read ↗

Structure and function of the ROR2 cysteine-rich domain in vertebrate noncanonical WNT5A signalingSemantic proximity Read ↗

RNF43 and ZNRF3 in Wnt Signaling - A Master Regulator at the MembraneSemantic proximity Read ↗

Non-canonical WNT/PCP signalling in cancer: Fzd6 takes centre stageSemantic proximity Read ↗

Structural basis for R-spondin recognition by LGR4/5/6 receptors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.