Motonori Matsusaki

OptoChaperone enables reversible, spatiotemporal control of protein condensates using light, demonstrating efficacy in regulating disease-related condensates without chemical additives or genetic modifications.

This study shows Ca2+ induces PDIA6 phase separation, enhancing proinsulin folding and preventing aggregation through recruitment of PDIA3.

This study investigates how the K76E mutation in PPIA affects protein dynamics and function, finding that it impairs isomerase activity through allosteric network disruption rather than structural changes.

This study identifies Kapβ2 as a target of DPRs, showing how DPR binding alters its phase-modifying function, leading to toxic RBP condensates in ALS models.

The paper compares how PDI and ERp46 recognize client proteins during oxidative folding, showing distinct mechanisms that influence disulfide bond formation and protein quality control.