This paper is the background for a new international formulation for the ion product of water substance (May 1980) issued by the International Association for the Properties of Steam. The ion product of water (Kw) is represented hy an equation, based on density and two 'lluH-1rJ'ltir. fllndion~ of reciprocal absolute temperature. for use from 0 to 1000°C and 1 to 10,000 bars pressure. The equation is believed to describe within ±0.01 units of log K: (where K: equals Kj(mol kg-I)2) many of the measurements at saturated vapor pressure up to 200°C, and to within ±0.02 units up to the critical temperature (374°C). It also describes within the experimental uncertainty the several sets of measurements at high pressures and should provide values within ±0.05 and 0.30 units at low and high temperatures, respectively.
Poxviruses encode proteins that suppress host immune responses, including secreted decoy receptors for pro-inflammatory cytokines such as interleukin-1 (IL-1) and the vaccinia virus proteins A46R and A52R that inhibit intracellular signaling by members of the IL-1 receptor (IL-1R) and Toll-like receptor (TLR) family. In vivo, the TLRs mediate the innate immune response by serving as pathogen recognition receptors, whose oligomerized intracellular Toll/IL-1 receptor (TIR) domains can initiate innate immune signaling. A family of TIR domaincontaining adapter molecules transduces signals from engaged receptors that ultimately activate NF-B and/or interferon regulatory factor 3 (IRF3) to induce proinflammatory cytokines. Data base searches detected a significant similarity between the N1L protein of vaccinia virus and A52R, a poxvirus inhibitor of TIR signaling. Compared with other poxvirus virulence factors, the poxvirus N1L protein strongly affects virulence in vivo; however, the precise target of N1L was previously unknown. Here we show that N1L suppresses NF-B activation following engagement of Toll/IL-1 receptors, tumor necrosis factor receptors, and lymphotoxin receptors. N1L inhibited receptor-, adapter-, TRAF-, and IKK-␣ and IKK--dependent signaling to NF-B. N1L associated with several components of the multisubunit I-B kinase complex, most strongly associating with the kinase, TANK-binding kinase 1 (TBK1). Together these findings are consistent with the hypothesis that N1L disrupts signaling to NF-B by Toll/IL-1Rs and TNF superfamily receptors by targeting the IKK complex for inhibition. Furthermore, N1L inhibited IRF3 signaling, which is also regulated by TBK1. These studies define a role for N1L as an immunomodulator of innate immunity by targeting components of NF-B and IRF3 signaling pathways.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.