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Masatomo So

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Biochimica Et Biophysica Acta. Proteins and Proteomics|December 28, 2020
Carbonyl <sup>13</sup>C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to β<sub>2</sub>-microglobulinYuichi Yoshimura, Masatomo So, Yohei Miyanoiri
Current Opinion in Structural Biology|January 18, 2016
Revisiting supersaturation as a factor determining amyloid fibrillationMasatomo So, Damien Hall, Yuji Goto
The Journal of Biological Chemistry|August 24, 2019
Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregationKenji Sasahara, Keiichi Yamaguchi, Masatomo So, et al.
FEBS Letters|May 21, 2026
Degradation mechanism of the von Willebrand factor A2 domain by nattokinaseRyuichi Hyakumoto, Masatomo So, Ayako Furukawa, et al.
Protein Science : a Publication of the Protein Society|March 2, 2017
Heparin-induced amyloid fibrillation of β<sub>2</sub> -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagramMasatomo So, Yasuko Hata, Hironobu Naiki, et al.
The Journal of Biological Chemistry|August 14, 2014
High-throughput analysis of ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the large fluctuation in the lag timeAyaka Umemoto, Hisashi Yagi, Masatomo So, et al.
Biophysical Reviews|December 20, 2017
Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanismYuji Goto, Masayuki Adachi, Hiroya Muta, et al.
Biomolecular NMR Assignments|March 23, 2026
<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone resonance assignments of the A2 domain of human von Willebrand factorRyuichi Hyakumoto, Masatomo So, Ayako Furukawa, et al.
Biomolecular NMR Assignments|May 29, 2026
Backbone resonance assignments of CPEB3 [1-120], CPEB3 [186-315], and CPEB3 [400-459]Yujin Lee, Harunobu Saito, Masatomo So, et al.
The Journal of Biological Chemistry|June 12, 2015
Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid FibrillationMasayuki Adachi, Masatomo So, Kazumasa Sakurai, et al.
Pageof 7

Showing results (1-10 of 66) with videos related to

Sort By:
Pageof 7
Biochimica Et Biophysica Acta. Proteins and Proteomics|December 28, 2020
Carbonyl <sup>13</sup>C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to β<sub>2</sub>-microglobulinYuichi Yoshimura, Masatomo So, Yohei Miyanoiri
Current Opinion in Structural Biology|January 18, 2016
Revisiting supersaturation as a factor determining amyloid fibrillationMasatomo So, Damien Hall, Yuji Goto
The Journal of Biological Chemistry|August 24, 2019
Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregationKenji Sasahara, Keiichi Yamaguchi, Masatomo So, et al.
FEBS Letters|May 21, 2026
Degradation mechanism of the von Willebrand factor A2 domain by nattokinaseRyuichi Hyakumoto, Masatomo So, Ayako Furukawa, et al.
Protein Science : a Publication of the Protein Society|March 2, 2017
Heparin-induced amyloid fibrillation of β<sub>2</sub> -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagramMasatomo So, Yasuko Hata, Hironobu Naiki, et al.
The Journal of Biological Chemistry|August 14, 2014
High-throughput analysis of ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the large fluctuation in the lag timeAyaka Umemoto, Hisashi Yagi, Masatomo So, et al.
Biophysical Reviews|December 20, 2017
Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanismYuji Goto, Masayuki Adachi, Hiroya Muta, et al.
Biomolecular NMR Assignments|March 23, 2026
<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone resonance assignments of the A2 domain of human von Willebrand factorRyuichi Hyakumoto, Masatomo So, Ayako Furukawa, et al.
Biomolecular NMR Assignments|May 29, 2026
Backbone resonance assignments of CPEB3 [1-120], CPEB3 [186-315], and CPEB3 [400-459]Yujin Lee, Harunobu Saito, Masatomo So, et al.
The Journal of Biological Chemistry|June 12, 2015
Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid FibrillationMasayuki Adachi, Masatomo So, Kazumasa Sakurai, et al.
Pageof 7