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Toxins|February 9, 2021
pH-Dependent Protein Binding Properties of Uremic Toxins In VitroSuguru Yamamoto, Kenichi Sasahara, Mio Domon, et al.
The Journal of Biological Chemistry|February 12, 2020
Inorganic polyphosphate potentiates lipopolysaccharide-induced macrophage inflammatory responseToru Ito, Suguru Yamamoto, Keiichi Yamaguchi, et al.
Ultrasonics Sonochemistry|March 26, 2021
Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentationKichitaro Nakajima, Kentaro Noi, Keiichi Yamaguchi, et al.
The Journal of Biological Chemistry|September 10, 2019
Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pHMasahiro Noji, Kenji Sasahara, Keiichi Yamaguchi, et al.
Biochemistry|August 28, 2018
Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin PolymerizationMasahiro Noji, Masatomo So, Keiichi Yamaguchi, et al.
ACS Sensors|June 26, 2023
Ultrastiff Amyloid-Fibril Network of α-Synuclein Formed by Surface Seeding Reaction Confirmed by Multichannel Electrodeless Quartz-Crystal-Microbalance BiosensorLianjie Zhou, Touko Hajiri, Kichitaro Nakajima, et al.
Nutrients|December 23, 2023
Sodium L-Aspartate Supplementation Improves Repeated-Sprint PerformanceKeiichi Yamaguchi, Nanako Hayashi, Daichi Sumi, et al.
Protein Science : a Publication of the Protein Society|May 28, 2021
Polyphenol-solubility alters amyloid fibril formation of α-synucleinMasatomo So, Yuto Kimura, Keiichi Yamaguchi, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 12, 2019
Possible mechanisms of polyphosphate-induced amyloid fibril formation of β2-microglobulinChun-Ming Zhang, Keiichi Yamaguchi, Masatomo So, et al.
Current Research in Structural Biology|July 8, 2021
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanismKoki Furukawa, Cesar Aguirre, Masatomo So, et al.
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