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Journal: Nature Communications
Article Title: Structural studies of the IFNλ4 receptor complex using cryoEM enabled by protein engineering
doi: 10.1038/s41467-025-56119-y
Figure Lengend Snippet: A pSTAT1 signaling of IFNω1 (orange), IFNλ3 (blue), and IFNλ4 (red) in Hap1 cells. Curves are fit to a first-order logistic model. Data are presented with mean values and error bars representing ±SEM ( n = 3 biologically independent experiments). B Relative quantification (RQ) of select genes induced by IFNω1, IFNλ3, and IFNλ4 in Hap1 cells treated with saturating concentrations (100 nM) interferon for 6 h as measured by qPCR. Data are presented with mean values. Error bars represent 95% confidence intervals ( n = 3 biologically independent experiments). C Changes in induction of ISG15 or MX1 over time for IFNλ3 and IFNλ4 in Huh7.5.1 cells at a range of concentrations (~0.5, 1.5, 5, and 15 nM). Statistical significance determined by a two-tailed student t -test. Data are presented as mean values ± SD ( n = 3 biologically independent experiments; * = p ≤ 0.05, ** = p ≤ 0.01, *** = p ≤ 0.001). D Intracellular HCV genomic RNA level over time following treatment with IFNω1, IFNλ3, or IFNλ4 in Huh7.5.1 cells. Statistical significance was determined by a two-tailed student t -test. Data are presented as mean values ± SD ( n = 3 biologically independent experiments; * = p ≤ 0.05, ** = p ≤ 0.01).
Article Snippet: To quantify activation of pSTAT1, cells were washed thrice with 0.5% PBSA and then stained with an
Techniques: Quantitative Proteomics, Two Tailed Test