D. M. Lawson

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.

This paper reports the crystal structures of SAP05 complexes and reveals their bimodular architecture enabling ubiquitin-independent targeted protein degradation in eukaryotic cells.

A helper NLR is mutated to evade inhibition by a parasite effector, restoring disease resistance gene activity.

The paper reports the crystal structure of an ADH enzyme that catalyzes a non-canonical 1,4 reduction, providing insights into how plant ADHs diversify their catalytic functions.

This paper reveals how the blast fungus effector AVR-Pii binds to rice Exo70, modulating immune recognition through a novel Zinc-finger fold and conserved hydrophobic interface.

The paper solves the structure of a truncated Bacillus subtilis Noc protein bound to NBS DNA, revealing disengagement between its CTP-binding and DNA-binding domains.

This study identifies a CTP-dependent gating mechanism in ParB that regulates its nucleation, spreading, and recycling during chromosome segregation in Caulobacter crescentus.

This study shows that CTP regulates the membrane-binding activity of the nucleoid occlusion protein Noc in Bacillus subtilis by controlling its ability to form nucleoprotein complexes.

The paper reconstructs the evolutionary history of rice NLR receptors Pik-1 and Pik-2, showing their HMA domain evolved convergent high-affinity binding to the fungal effector AVR-PikD.

This study investigates how DNA-binding specificity diversifies in ParB and Noc proteins by identifying key residues and mutational paths that reprogram specificity.