He Zhao

This study investigates the oligomerization and activation mechanism of the RPS4-RRS1 immune receptor complex in Arabidopsis, showing that effector recognition triggers conformational changes that enable NADase activity.

The paper identifies two resistance genes from Solanum americanum that confer resistance to Phytophthora pathogens and shows their NLR cluster evolves in response to multiple pathogens.

The paper identifies Rladg, a potato TIR-NLR receptor that confers broad-spectrum resistance to poleroviruses by recognizing conserved protease structures.

The paper shows that NLR immune receptor architecture enforces EDS1-dependency on diverse TIR domains in plants.

Activated wheat CCG10-NLR immune receptor WAI3 and Arabidopsis RPS2 assemble into octameric calcium-permeable resistosomes with an inverted coiled-coil domain topology associated with lacking the conserved EDVID motif.

This study determines the structural basis of broad recognition by the Arabidopsis NLR WRR4A, revealing a shape-based mechanism that enables recognition of diverse effectors with similar three-dimensional architectures.

This study shows how the helper NLR NRC2 converts from a homodimer to a higher-order oligomer upon activation by the sensor NLR Rx, revealing the molecular mechanism of plant immune activation.

The paper shows that reducing glial genes involved in synaptic function reduces disease pathology and behavioral issues in a Drosophila Huntington's Disease model.