Sort   by:  
 Page size 
ProteomicsZNRF3 and RNF43 are active monomeric E3 ligases that self-associate
Crosslinking mass spectrometry was used to identify the site of dimerization in the RING domain of ZNRF3. The two proteins, ZNRF3 and RNF43 have a key role in regulating the number of Frizzled (FZD) receptor on cells and their inactivation causes cancer. This is because they are RING E3 ligases that...
ORGANISM(S): Homo sapiens (Human) 
2026-07-30 | PXD070424 | Pride
Znrf3 e3 ligase Cross-linking Ring dimerization 
GenomicsPotent and selective binders of the E3 ubiquitin ligase ZNRF3 stimulate Wnt signaling and intestinal organoid growth
Potent and selective binders of the E3 ubiquitin ligase ZNRF3 stimulate Wnt signaling and intestinal organoid growth
PRJNA1022399 | ENA
ProteomicsStructure-guided development of chemically tailored peptide binders of RNF43/ZNRF3 to enable versatile design of membrane protein-targeting PROTACs
Targeted membrane protein degradation using cell surface E3 ligases RNF43/ZNRF3 via proteolysis targeting chimeras (PROTACs) represents an effective strategy for treating membrane drug targets that cannot be fully inhibited using traditional inhibitors. Several ingenious chimeras have been developed...
ORGANISM(S): Homo Sapiens 
2025-03-04 | PXD061425 |
OtherPotent and selective binders of the E3 ubiquitin ligase ZNRF3 stimulate Wnt signaling and intestinal organoid growth
Selective and precise activation of signaling transduction cascades is key for cellular reprogramming and tissue regeneration. However, the development of small or large molecule agonists for many signaling pathways has remained elusive and is rate limiting to realize the full clinical potential of ...
ORGANISM(S): Homo sapiens 
2024-09-28 | GSE244316 | GEO
UnknownSCFβ-TRCP E3 ubiquitin ligase targets the tumor suppressor ZNRF3 for ubiquitination and degradation.
Not available
S-EPMC6160385 | biostudies-literature
UnknownStructural and molecular basis of ZNRF3/RNF43 transmembrane ubiquitin ligase inhibition by the Wnt agonist R-spondin.
Not available
S-EPMC3905715 | biostudies-literature
UnknownMiR-668-5p targets ZNRF3, an E3 ubiquitin ligase to enhance osteoblast function and alleviate senescence in doxorubicin-induced age-related bone loss.
Not available
S-EPMC12597718 | biostudies-literature
ProteomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
The majority of current therapeutics targeting plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. Typical mammalian proteins, however, consist of multiple domains executing discrete but coordinated activities, and saturating inhibition of one functional domain...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-05-25 | MSV000089542 | MassIVE
UnknownLoss of ZNRF3/RNF43 Unleashes EGFR in Cancer.
Not available
S-EPMC10802575 | biostudies-literature
UnknownReceptor Elimination by E3 Ubiquitin Ligase Recruitment (REULR): A Targeted Protein Degradation Toolbox.
Not available
S-EPMC10127277 | biostudies-literature
Sort   by:  
 Page size