Hayden Burdett

This study identifies a novel N-terminal region in TET1 that binds nucleosomes, enabling chromatin association in mouse embryonic stem cells through structural and biochemical validation.

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.

This study determines the structure of H3.V-H4.V nucleosomes in Trypanosoma brucei and shows how these variants promote nucleosome plasticity in repressed chromatin.

The paper determines cryo-EM structures of a plant TNL NLR, revealing its activation mechanism and NAD+ recognition, which informs engineering disease-resistant crops.

This study identifies tetramerisation as essential for SALL transcription factor function, showing its role in DNA binding and linking it to developmental disorders.

This study identifies the N-terminal region of DNMT3A as containing multiple chromatin-binding motifs that mediate recruitment through interactions with nucleosomes and ubiquitylated histone H2AK119.

This study investigates how the BRCA1-BARD1 complex interacts with chromatin containing specific histone modifications, showing it preferentially binds di-nucleosomes and uses multivalent interactions to overcome inhibitory marks.