pathway were tested using the A549/pr .GFP reporter cell-line. The IFN induction pathway and hence GFP expression was optimally activated in this cell-line by infection with a PIV-5/VDC virus stock rich in DIs . Inhibitors that target components of the IFN induction pathway would be expected to block GFP expression. The IKK-2 inhibitor TPCA-1 demonstrated a significant block to GFP expression, while the TBK1 inhibitor BX795 showed a weak effect at a concentration of 4 mM, however no activity was observed for the MRT68844 and MRT67307 inhibitors . The JAK1 inhibitors were similarly tested in the A549/pr .GFP reporter cell-line following activation of the IFN signaling pathway using purified IFN . All four JAK1 inhibitors blocked GFP expression in the .GFP reporter cell-line, however Ruxolitinib had the greatest effect . Therefore six of the molecules tested inhibited the IFN induction or IFN signaling pathway as expected without causing cellular cytotoxicity , however the two MRT molecules did not show any activity in this cell-based assay. Effect of the inhibitors on viral Glesatinib (hydrochloride) plaque formation was examined using A549 cells infected with GW-610742 recombinant Bunyamwera virus , in which the NSs IFN antagonist has been inactivated rendering the virus IFN sensitive . During direct interaction with 7-nAChRs, Ric-3 may recruit other proteins to the receptor complex to facilitate surface expression. After the dissociation of Ric-3, proteins may associate with mature 7-nAChRs as a result of Ric-3-mediated surface expression. The comparison of 7-nAChR complexes from SH-EP1-h7-Ric-3 and SH-EP1-h7 cells provides a method of identifying associated proteins, including those that may be essential for Ric- 3-mediated enhancement of 7-nAChR surface expression. Cells were washed with homogenization buffer before being mechanically dislodged. Isolated cells were then homogenized with 30 strokes of a Potter-Elvehjem glass homogenizer on ice. SH-EP1-h7-Ric-3, SH-EP1-h7 and SH-EP1 membrane solubilization conditions were adapted. Membrane fragments were isolated following centrifugation. Membrane pellets were then homogenized in solubilization buffer with strokes of a Potter-Elvehjem glass homog
