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 role of the cysteine-rich domain of Frizzled in Wingless-Armadillo signaling.

The EMBO journal - 5 Oct 2005

Povelones Michael, Nusse Roel

Abstract excerpt

The Frizzled (Fz) receptors contain seven transmembrane helices and an amino-terminal cysteine-rich domain (CRD) that is sufficient and necessary for binding of the ligands, the Wnts. Recent genetic experiments have suggested, however, that the CRD is dispensable for signaling. We engineered fz CRD mutant transgenes and tested them for Wg signaling activity. None of the mutants was functional in cell culture or...

Read the complete abstract on PubMed

Topics

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

Share to Armadillo Domain Proteins
Share to Cysteine
Share to Frizzled Receptors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Receptors, G-Protein-Coupled

Share to RNA Interference

Share to Transgenes

Share to Wings, Animal

Share to Wnt1 Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 16163385
DOI: 10.1038/sj.emboj.7600817
PMCID: PMC1276175

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 role of the cysteine-rich domain of Frizzled in Wingless-Armadillo signaling.PMID 16163385Read ↗

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

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

Wingless transduction by the Frizzled and Frizzled2 proteins of Drosophila.Semantic proximity Read ↗

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

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

Transducing properties of Drosophila Frizzled proteins.Semantic proximity Read ↗

Signaling specificity by Frizzled receptors in Drosophila.Semantic proximity Read ↗

The conserved transmembrane RING finger protein PLR-1 downregulates Wnt signaling by reducing Frizzled, Ror and Ryk cell-surface levels in C. elegans.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 ↗

Quantitative Profiling of WNT-3A Binding to All Human Frizzled Paralogues in HEK293 Cells by NanoBiT/BRET AssessmentsSemantic proximity Read ↗

A regulatory receptor network directs the range and output of the Wingless signal.Semantic proximity Read ↗

Clarifying Frizzled 2 function in development through genetically validated mouse models.Semantic proximity Read ↗

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