Blair R. Renshaw

TL;DR: Aberrant interleukin-36Ra structure and function lead to unregulated secretion of inflammatory cytokines and generalized pustular psoriasis.

TL;DR: It is demonstrated that IL-1F6 and IL- 1F8, in addition to IL-2F9, activate the pathway leading to NF-κB in an IL-3Rrp2-dependent manner in Jurkat cells as well as in multiple other human and mouse cell lines, and thatIL-1RrP2 antibodies block activation of the pathwayLeading to NF -κB by IL-0F6, IL-8, and Il-1

TL;DR: The cloning and characterization of four new members of the interleukin-1 (IL-1) family (FIL1δ, FIL1ε, Fil1ζ, and FIL1η, with FIL1 standing for “Family of IL-1”) are reported here.

TL;DR: It is demonstrated that IL-36Ra antagonist activity is dependent upon removal of its N-terminal methionine, and the mechanism of action is directly analogous to that of IL-1Ra, which suggests that protease(s) that activate IL- 36 cytokines could be excellent drug targets for psoriasis.

TL;DR: It is concluded that the SIGIRR protein represents a novel subtype of the IL-1R superfamily, which has only one Ig domain in its extracellular portion and an unusually long cytoplasmic domain is reminiscent of the structure of drosophila Toll.