@misc{oai:repo.qst.go.jp:00077259,
 author = {Fujiwara, Satoru and Matsuo, Tatsuhito and Sugimoto, Yasunobu and Fujiwara, Satoru and Matsuo, Tatsuhito},
 month = {Sep},
 note = {Formation of amyloid fibrils of α-synuclein αSyn) is closely related to the pathogenesis of Parkinson's disease. Structural analysis of amyloid fibrils is important for elucidation of the mechanism of the fibril formation, and thus elucidation of the mechanism of the pathogenesis. Here we characterize the structure of amyloid fibrils of αSyn by small-angle X-ray and neutron scattering (SAXS and SANS), in particular, the structure of αSyn within fibrils. In addition to the information on the shape and the hydration structure of fibrils obtained from the combined analysis of SAXS and SANS, the information on the structure of individual αSyn within fibrils was obtained using the new SANS method. Comparison with the structure of αSyn in the monomeric state is discussed., 第57回日本生物物理学会年会},
 title = {Structural analysis of human α-synuclein within amyloid fibrils by small-angle scattering},
 year = {2019}
}