Azita Leavitt

The paper identifies a bacterial defense mechanism, aRES, that depletes NAD+ by producing ADPR-1P, which resists phage NARP1 reconstitution, and describes phage countermeasures including phosphatases and inhibitors.

This study shows that TIR domains in animals, including human TLR4, have conserved catalytic activity that produces cADPR and is essential for TLR4 signaling.

The paper systematically identifies TIR-based immune signaling systems in bacteria, finding they exist in 8% of bacterial genomes and use signaling molecules similar to those in plant and human immunity.

The paper identifies His-ADPR as a novel TIR-derived immune signaling molecule in bacteria, showing its role in phage defense and structural basis for recognition.

This study identifies a bacterial immune system where TIR-domain proteins activate caspase-like proteases to induce cell death and block phage replication.

This study identifies anti-defense proteins in phages that inhibit bacterial immune systems like Gabija, Thoeris, and Hachiman.