J. P. Mackay

The paper discovers and characterizes cyclic peptides that selectively bind to the C-terminal bromodomains of BET family proteins, showing high potency and paralogue-specificity.

The paper combines cross-linking mass spectrometry with AI-based structure prediction to discover and validate protein and complex structures at proteome scale.

This study determines the molecular architecture of three NuRD sub-complexes using integrative structural methods, revealing new subunit interfaces and MBD3 localization.

The paper identifies paralogue-specific protein interactions of the MGCC module in the NuRD complex, revealing mechanisms for functional specificity and integration into other complexes.

This study reveals the asymmetric and dynamic architecture of the NuRD complex using integrated biochemical and structural methods.

The paper identifies high-affinity, specific cyclic peptide inhibitors of BET bromodomains using RaPID screening, revealing diverse binding modes and structures.

This study identifies hemophilin, a heme-binding protein from Haemophilus haemolyticus, which inhibits non-typeable Haemophilus influenzae by heme starvation.