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Showing 1–4 of 4 results

Advanced filters: Author: Matthias Zebisch Clear advanced filters

Structural and molecular basis of ZNRF3/RNF43 transmembrane ubiquitin ligase inhibition by the Wnt agonist R-spondin

R-spondins are secreted factors that potentiate Wnt signalling by inhibiting the degradation of Wnt receptors by transmembrane E3 ubiquitin ligases. Zebisch et al.present a panel of crystal structures that reveal how this inhibition occurs.

Matthias Zebisch
Yang Xu
E. Yvonne Jones
ResearchOpen Access14 Nov 2013
Nature Communications

Volume: 4, P: 1-12
Notum deacylates Wnt proteins to suppress signalling activity

The biochemical activity of Notum as a carboxylesterase that removes an essential lipid moiety from Wnt proteins is uncovered; the interaction of Notum with glypicans is required to ensure localization at the cell surface, and Notum may provide a new target for therapeutic development in diseases with defective Wnt signalling.

Satoshi Kakugawa
Paul F. Langton
Jean-Paul Vincent
Research25 Feb 2015
Nature

Volume: 519, P: 187-192
Structural insights into selective small molecule activation of PKG1α

Structural characterization and modeling of cGMP‐dependent protein kinase I‐α (PKG1α) with a small molecule activator suggest the activation mechanism for the PKG1α homodimer.

Essam Metwally
Victor Mak
Thierry O. Fischmann
ResearchOpen Access31 Jul 2023
Communications Biology

Volume: 6, P: 1-13
Crystal structure and substrate binding mode of ectonucleotide phosphodiesterase/pyrophosphatase-3 (NPP3)

Christoph Döhler
Matthias Zebisch
Norbert Sträter
ResearchOpen Access18 Jul 2018
Scientific Reports

Volume: 8, P: 1-13