Z.-Y. Guo

The paper engineers a bamboo-derived peptide ligase with improved activity by modifying its activation mechanism.

The study identifies that GHSR in coelacanth binds and is activated by motilin, while zebrafish and large yellow croaker GHSRs do not bind motilin, suggesting ancient fish GHSRs had two agonists.

The paper shows that FAM237B activates GPR83 at nanomolar concentrations, confirming it as an endogenous agonist.

This study identifies FAM237A as the true ligand of GPR83, refuting previous claims that PEN and proCCK56-63 are agonists of this receptor.

The paper shows LEAP2 binds more consistently to fish GHSRs than ghrelin, suggesting LEAP2 is a more conserved ligand in these species.

This study develops esterase-resistant and highly active ghrelin analogs using thiol-ene click chemistry, showing improved stability and activity in serum.

The paper develops a bioluminescent assay to identify and characterize peptide ligases, finding that several plant species likely express these enzymes.