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Journal Articles

Dynamic properties of human $$alpha$$-synuclein related to propensity to amyloid fibril formation

Fujiwara, Satoru*; Kono, Fumiaki*; Matsuo, Tatsuhito*; Sugimoto, Yasunobu*; Matsumoto, Tomoharu*; Narita, Tetsuhiro*; Shibata, Kaoru

Journal of Molecular Biology, 431(17), p.3229 - 3245, 2019/08

 Times Cited Count:14 Percentile:54.27(Biochemistry & Molecular Biology)

$$alpha$$-synuclein ($$alpha$$Syn) is an intrinsically disordered protein (IDP) with unknown function. $$alpha$$Syn is known to form amyloid fibrils, which are implicated with the pathogenesis of Parkinson's disease and other synucleinopathies. Elucidating the mechanism of fibril formation of $$alpha$$Syn is therefore important for understanding the mechanism of the pathogenesis of these diseases. Here, using the quasielastic neutron scattering (QENS) and small-angle X-ray scattering (SAXS) techniques, we investigated the dynamic and structural properties of $$alpha$$Syn. These results imply that fibril formation of $$alpha$$Syn requires not only the enhanced local motions but also the segmental motions such that the proper inter-molecular interactions are possible.

Journal Articles

Chemical evolution of amino acid induced by soft X-ray with synchrotron radiation

Kaneko, Fusae*; Tanaka, Masahito*; Narita, Satoru*; Kitada, Tomo*; Matsui, Takahiro*; Nakagawa, Kazumichi*; Agui, Akane; Fujii, Kentaro; Yokoya, Akinari

Journal of Electron Spectroscopy and Related Phenomena, 144-147, p.291 - 294, 2005/06

 Times Cited Count:19 Percentile:64.47(Spectroscopy)

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