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Current Opinion in Structural Biology|January 18, 2016
Revisiting supersaturation as a factor determining amyloid fibrillationMasatomo So, Damien Hall, Yuji GotoAnalytical Biochemistry|July 20, 2016
Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methodsDamien Hall, Ran Zhao, Masatomo So, et al.Biophysical Reviews|December 23, 2016
Measurement of amyloid formation by turbidity assay-seeing through the cloudRan Zhao, Masatomo So, Hendrik Maat, et al.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.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.Protein Science : a Publication of the Protein Society|March 2, 2017
Heparin-induced amyloid fibrillation of β2 -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagramMasatomo So, Yasuko Hata, Hironobu Naiki, 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.Analytical Biochemistry|November 22, 2017
A new look at an old view of denaturant induced protein unfoldingDamien Hall, Akira R Kinjo, Yuji GotoThe Journal of Biological Chemistry|November 5, 2017
Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillationAyame Nitani, Hiroya Muta, Masayuki Adachi, 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 36