Analysis and experimental assessment of the sensitivity of stimulated Raman scattering microscopy

Ozeki Y., Dake F., Kajiyama S., et al. Analysis and experimental assessment of the sensitivity of stimulated Raman scattering microscopy. Optics Express, 17, 5, 3651. https://doi.org/10.1364/OE.17.003651

Highly sensitive spectral interferometric fourwave mixing microscopy near the shot noise limit and its combination with two-photon excited fluorescence microscopy

Isobe K., Ozeki Y., Kawasumi T., et al. Highly sensitive spectral interferometric fourwave mixing microscopy near the shot noise limit and its combination with two-photon excited fluorescence microscopy. Optics Express, 14, 23, 11204. https://doi.org/10.1364/OE.14.011204

Label-free imaging by stimulated parametric emission microscopy reveals a difference in hemoglobin distribution between live and fixed erythrocytes

Hieu M. Dang, Gen Omura, Toshiyuki Omano, Masatomo Yamagiwa, Shin'ichiro Kajiyama, Yasuyuki Ozeki, Kazuyoshi Itoh, and Kiichi Fukui "Label-free imaging by stimulated parametric emission microscopy reveals a difference in hemoglobin distribution between live and fixed erythrocytes," Journal of Biomedical Optics 14(4), 040506 (1 July 2009). https://doi.org/10.1117/1.320715

Structure and Functional Characterization of Vibrio parahaemolyticus Thermostable Direct Hemolysin*

Thermostable direct hemolysin (TDH) is a major virulence factor of Vibrio parahaemolyticus that causes pandemic foodborne enterocolitis mediated by seafood. TDH exists as a tetramer in solution, and it possesses extreme hemolytic activity. Here, we present the crystal structure of the TDH tetramer at 1.5 Å resolution. The TDH tetramer forms a central pore with dimensions of 23 Å in diameter and ∼50 Å in depth. π-Cation interactions between protomers comprising the tetramer were indispensable for hemolytic activity of TDH. The N-terminal region was intrinsically disordered outside of the pore. Molecular dynamic simulations suggested that water molecules permeate freely through the central and side channel pores. Electron micrographs showed that tetrameric TDH attached to liposomes, and some of the tetramer associated with liposome via one protomer. These findings imply a novel membrane attachment mechanism by a soluble tetrameric pore-forming toxin