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 | 345 | 2012 |
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 | 90 | 2011 |
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 | 75 | 2016 |
Revisiting supersaturation as a factor determining amyloid fibrillation M So, D Hall, Y Goto Current Opinion in Structural Biology 36, 32-39, 2016 | 72 | 2016 |
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 | 71 | 2015 |
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 | 50 | 2017 |
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 | 50 | 2014 |
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 | 45 | 2013 |
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 | 44 | 2018 |
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 | 42 | 2016 |
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 | 42 | 2013 |
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 | 40 | 2019 |
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 | 39 | 2021 |
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 | 38 | 2018 |
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 | 37 | 2019 |
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 | 37 | 2017 |
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 | 28 | 2017 |
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 | 28 | 2017 |
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 | 27 | 2015 |
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 | 25 | 2020 |