K. Yokoyama

The paper uses cryo-EM to capture catalytic intermediates of ATP synthase F1 domain, revealing how ATP hydrolysis couples to mechanical rotation in 120-degree steps.

The paper identifies intermediate structures of V/A-ATPase during ATP activation using cryo-EM, showing how the ground-state structure transitions to steady-state through sequential ATP binding.

This paper introduces a rapid and universal LC-MS-based platform for quantifying monoclonal antibodies, offering a scalable alternative to traditional ligand binding assays.

The paper determines atomic models of V/A-ATPase catalytic intermediates, revealing a ratchet-like mechanism for unidirectional rotation instead of a power stroke model.

The paper determines the cryo-EM structures of holo V/A-ATPase and isolated Vo to elucidate the auto-inhibited form of Vo and its regulation of proton conductance.

This paper characterizes the kinetics of the radical-mediated C-C bond formation in MoaA, revealing a shunt pathway and determining the rate of the 3',8-cyclization step.