Margaret M. Stratton

The paper develops sensitive FRET biosensors to visualize CaMKII activity dynamics in living cells and demonstrates their use in cultured and primary cells, including neurons and cardiomyocytes.

This paper introduces SidBait, a modular proximity ligation approach to identify small molecule and protein targets, validated with known interactions and applied to discover new targets like CaMKII and CapZ.

This study identifies a domain-swapped conformation in CaMKII that enables linker-mediated allosteric regulation, demonstrated through structural, computational, and live-cell analyses.

This study identifies a novel feed-forward signalling axis between PEAK1 and CAMK2 in TNBC, showing that targeting CAMK2 can inhibit PEAK1-driven oncogenic processes.

This study determines the cryo-EM structure of the Nipah virus polymerase complex and identifies key domains critical for replication and transcription.

The paper identifies novel endogenous CAMK2 substrates by analyzing phosphoproteomic data from double knockout mice.

This paper investigates how PIPA, a GHB analog, affects CaMKII hub domain conformation and stability, revealing a mechanism involving Trp403 flip and hub domain stacking that reduces kinase activity.

This study investigates the oligomeric states and stability of CaMKIIalpha and CaMKIIbeta hub domains, revealing differences in their stoichiometry and stability in solution.

The paper develops a genetically encoded sensor, FRESCA, for measuring endogenous CaMKII activity, showing it captures aggregate activity across multiple variants unlike existing sensors.