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Article summary:
1. Two groups have studied the structures of two NLRs that carry Toll-like interleukin-1 receptor (TIR) domains (TIR-NLRs).
2. Upon recognition of pathogen invasion, NLRs trigger an immune response that resolves in a variety of ways depending on the type of NLR being activated.
3. The structure of the ROQ1-XopQ complex reveals that ROQ1 forms a tetrameric resistosome upon recognizing XopQ, and binding of the ROQ1 LRR to XopQ occurs through surface-exposed residues.
Article analysis:
The article is generally reliable and trustworthy, as it provides detailed information about the structure of two NLRs that carry Toll-like interleukin-1 receptor (TIR) domains (TIR-NLRs), and how they respond to pathogen invasion. The article also provides a clear explanation of how these TIR domains are activated by binding to the pathogen effector, which initiates NAD hydrolysis and begins the immune response.
However, there are some potential biases in the article that should be noted. For example, while it does provide detailed information about how these TIR domains are activated, it does not explore any possible risks associated with this activation or any potential side effects. Additionally, while it does provide an explanation for how recognition of the pathogen effector initiates NAD hydrolysis and begins the immune response, it does not provide any evidence to support this claim or explore any counterarguments. Furthermore, while it does provide a clear explanation for how binding of the ROQ1 LRR to XopQ occurs through surface-exposed residues, it does not explore any other possible mechanisms for this interaction or consider any other factors that may be involved in this process.
In conclusion, while overall reliable and trustworthy, there are some potential biases in this article that should be noted when considering its trustworthiness and reliability.