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Masatomo So
Masatomo So
Institute for Protein Research, Osaka University
在 protein.osaka-u.ac.jp 的电子邮件经过验证
标题
引用次数
引用次数
年份
Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation
Y Yoshimura, Y Lin, H Yagi, YH Lee, H Kitayama, K Sakurai, M So, H Ogi, ...
Proceedings of the National Academy of Sciences 109 (36), 14446-14451, 2012
3452012
Ultrasonication-dependent acceleration of amyloid fibril formation
M So, H Yagi, K Sakurai, H Ogi, H Naiki, Y Goto
Journal of molecular biology 412 (4), 568-577, 2011
902011
Measurement of amyloid formation by turbidity assay—seeing through the cloud
R Zhao, M So, H Maat, NJ Ray, F Arisaka, Y Goto, JA Carver, D Hall
Biophysical reviews 8, 445-471, 2016
752016
Revisiting supersaturation as a factor determining amyloid fibrillation
M So, D Hall, Y Goto
Current Opinion in Structural Biology 36, 32-39, 2016
722016
Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation
M Adachi, M So, K Sakurai, J Kardos, Y Goto
Journal of Biological Chemistry 290 (29), 18134-18145, 2015
712015
Model membrane size-dependent amyloidogenesis of Alzheimer's amyloid-β peptides
M Kinoshita, E Kakimoto, MS Terakawa, Y Lin, T Ikenoue, M So, T Sugiki, ...
Physical Chemistry Chemical Physics 19 (24), 16257-16266, 2017
502017
High-throughput analysis of ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the large fluctuation in the lag time
A Umemoto, H Yagi, M So, Y Goto
Journal of Biological Chemistry 289 (39), 27290-27299, 2014
502014
Ultrasonication: an efficient agitation for accelerating the supersaturation-limited amyloid fibrillation of proteins
Y Yoshimura, M So, H Yagi, Y Goto
Japanese Journal of Applied Physics 52 (7S), 07HA01, 2013
452013
Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism
Y Goto, M Adachi, H Muta, M So
Biophysical reviews 10, 493-502, 2018
442018
A small-angle X-ray scattering study of alpha-synuclein from human red blood cells
K Araki, N Yagi, R Nakatani, H Sekiguchi, M So, H Yagi, N Ohta, Y Nagai, ...
Scientific reports 6 (1), 30473, 2016
422016
A common mechanism underlying amyloid fibrillation and protein crystallization revealed by the effects of ultrasonication
H Kitayama, Y Yoshimura, M So, K Sakurai, H Yagi, Y Goto
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1834 (12), 2640-2646, 2013
422013
Possible mechanisms of polyphosphate-induced amyloid fibril formation of β2-microglobulin
C Zhang, K Yamaguchi, M So, K Sasahara, T Ito, S Yamamoto, I Narita, ...
Proceedings of the National Academy of Sciences 116 (26), 12833-12838, 2019
402019
Breakdown of supersaturation barrier links protein folding to amyloid formation
M Noji, T Samejima, K Yamaguchi, M So, K Yuzu, E Chatani, ...
Communications Biology 4 (1), 120, 2021
392021
Aggregation-phase diagrams of β2-microglobulin reveal temperature and salt effects on competitive formation of amyloids versus amorphous aggregates
M Adachi, M Noji, M So, K Sasahara, J Kardos, H Naiki, Y Goto
Journal of Biological Chemistry 293 (38), 14775-14785, 2018
382018
Ultrasonication-based rapid amplification of α-synuclein aggregates in cerebrospinal fluid
K Kakuda, K Ikenaka, K Araki, M So, C Aguirre, Y Kajiyama, K Konaka, ...
Scientific Reports 9 (1), 6001, 2019
372019
Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation
A Nitani, H Muta, M Adachi, M So, K Sasahara, K Sakurai, E Chatani, ...
Journal of Biological Chemistry 292 (52), 21219-21230, 2017
372017
Heparin‐induced amyloid fibrillation of β2‐microglobulin explained by solubility and a supersaturation‐dependent conformational phase diagram
M So, Y Hata, H Naiki, Y Goto
Protein Science 26 (5), 1024-1036, 2017
282017
Drastic acceleration of fibrillation of insulin by transient cavitation bubble
K Nakajima, D Nishioka, M Hirao, M So, Y Goto, H Ogi
Ultrasonics Sonochemistry 36, 206-211, 2017
282017
Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils
H Yagi, A Mizuno, M So, M Hirano, M Adachi, Y Akazawa-Ogawa, ...
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1854 (3), 209-217, 2015
272015
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism
K Furukawa, C Aguirre, M So, K Sasahara, Y Miyanoiri, K Sakurai, ...
Current Research in Structural Biology 2, 35-44, 2020
252020
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