P. Ann Boriack-Sjodin

TL;DR: The results indicate that structure‐based computational design can be successfully applied to further improve the binding of high‐affinity antibodies and improve the single‐mutant success rate.

TL;DR: The first detailed report of a TβRI kinase small molecule co-complex confirms the predicted binding interactions of the small molecule inhibitor, which stabilizes the inactive kinase conformation.

TL;DR: About one-third of the Shh surface can be modified without effect on function regardless of the size of the attachment, indicating that the interaction of Shh with its primary receptor Ptc is mediated over a large surface of theShh protein.

TL;DR: The results are the first to demonstrate the efficacy of an orally active, small-molecule ALK5/ALK4 inhibitor in a vascular fibrosis model and suggest the potential therapeutic application of these inhibitors inascular fibrosis.

TL;DR: In addition to mutations that decreased or disrupted binding, one antibody mutation resulted in a 70-fold increase in affinity for human MCP-2, and engineering the preferred residue into the chemokine conferred binding to the antibody.