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Published Erratum
. 2025 Mar 11;122(10):e2502122122.
doi: 10.1073/pnas.2502122122. Epub 2025 Feb 20.

Correction for Manik et al., Structural basis for TIR domain-mediated innate immune signaling by Toll-like receptor adaptors TRIF and TRAM

No authors listed
Published Erratum

Correction for Manik et al., Structural basis for TIR domain-mediated innate immune signaling by Toll-like receptor adaptors TRIF and TRAM

No authors listed. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 4.
Fig. 4.
Analysis of effects of mutations of residues in the TRAM:TRAM interaction interfaces on signaling efficiency. (A) MyD88 KO reporter cells were transiently transfected with 100 ng TRAM-GFP constructs (WT or mutants). On the following day, the cells were treated with or without 100 ng/mL LPS and incubated for 16 h. The cells were harvested and run on a flow cytometer. Cells expressing TRAM-GFP at a modest level were selected for analysis (SI Appendix, Fig. S5A). NF-κB-driven mScarlet-I reporter expression for each mutant was normalized to LPS-stimulated WT control (% WT + LPS). Results are from two to three independent experiments. Each dot indicates the mean of duplicates within an individual experiment. Note that WT controls were done 9 times, as they were included for every single experiment. ****P < 0.0001, ***P < 0.001, **P < 0.01, or *P < 0.05 compared to WT + LPS in one sample t test. (B) All the mutated residues are mapped on the TRAMTIR structure and highlighted according to their effect on the signaling. The blue lines represent the physical contact area between TRAMs (identified by using the PyMOL software); for BCD interfaces, the interactions with two molecules are shown by two different shades of blue line. Note that the effects of Q190A and M158R were chosen for those residues as more than one mutant was tested.

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