Beverly J. Castner

TL;DR: The results should facilitate the development of therapeutically useful inhibitors of TNF-α release, and they indicate that an important function of adamalysins may be to shed cell-surface proteins.

TL;DR: The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.

TL;DR: It is demonstrated that TACE (tumor necrosis factor α converting enzyme), a member of the ADAM family (a disintegrinand metalloprotease-family) of proteases, plays a central role in regulated α-cleavage of APP.

TL;DR: A broad role for TACE in the regulated shedding of EGFR ligands is supported, showing that cells lacking TACE activity shed dramatically less TGF-α as compared with wild-type cultures and that T GF-α cleavage was partially restored by infection of Tace-deficient cells with TACE-encoding adenovirus.

TL;DR: The structure of TACE opens a different approach toward the design of specific synthetic TACE inhibitors, which could act as effective therapeutic agents in vivo to modulate TNFalpha-induced pathophysiological effects, and might also help to control related shedding processes.