Martin F. Wolfson

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: The biologic activity ofIL-17 is dependent on a complex composed of IL-17RA and IL- 17RC, suggesting a new paradigm for understanding the interactions between the expanded family of IL -17 ligands and their receptors.

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.

TL;DR: In vitro whole cell panning approach using antibody phage display technology to identify cell-surface epitopes specifically expressed on human blood BDCA3+ DCs demonstrated that anti-1F12 scFv binds Nectin-like protein 2, an adhesion molecule involved in tumor suppression, synapse formation, and spermatogenesis, which defines a specialized subset of DCs in both mouse and human.