Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
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)-synuclein (Syn) is an intrinsically disordered protein (IDP) with unknown function. 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 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 Syn. These results imply that fibril formation of Syn requires not only the enhanced local motions but also the segmental motions such that the proper inter-molecular interactions are possible.
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)no abstracts in English