Masatomo So

Publication Activity (10 Years)

Years Active: 2018-2024
Publications (10 Years): 22

Top Topics

Multiple Myeloma

High Resolution

Single Molecule

Magnetic Resonance

Top Venues

Nature communications

The Journal of biological chemistry

Protein science : a publication of the Protein Society

This page only lists publications with an associated author ORCID identifier.

Publications

Masatomo So, Misaki Ono, Shigeki Oogai, Minako Kondo, Kaede Yamazaki, Charlotte Nachtegael, Hiroshi Hamajima, Risa Mutoh, Masaki Kato, Hisaya Kawate, Tomoyuki Oki, Yasushi Kawata, Shiho Kumamoto, Noritaka Tokui, Toshiki Takei, Kuniyoshi Shimizu, Akio Inoue, Naoki Yamamoto, Motoko Unoki, Kenichi Tanabe, Kinichi Nakashima, Hiroyuki Sasaki, Hironobu Hojo, Yasuo Nagata, Isao Suetake
Inhibitory effects of extracts from Eucalyptus gunnii on α-synuclein amyloid fibrils. Bioscience, biotechnology, and biochemistry (2024)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Martin Wilkinson, Rodrigo U Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D Aubrey, Sheena E Radford, Neil A Ranson
Disease-relevant β 2 -microglobulin variants share a common amyloid fold. Nature communications 14 (1) (2023)
Yuki Yoshikawa, Keisuke Yuzu, Naoki Yamamoto, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Tetsushi Iwasaki, Masatomo So, Yuji Goto, Atsuo Tamura, Eri Chatani
Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain. Molecules (Basel, Switzerland) 27 (13) (2022)
Ryosuke Tomiyama, Masatomo So, Keiichi Yamaguchi, Yohei Miyanoiri, Kazumasa Sakurai
The residual structure of acid-denatured β 2 -microglobulin is relevant to an ordered fibril morphology. Protein science : a publication of the Protein Society (2022)
Éva Bulyáki, Judit Kun, Tamás Molnár, Alexandra Papp, András Micsonai, Henrietta Vadászi, Borbála Márialigeti, Attila István Kovács, Gabriella Gellen, Keiichi Yamaguchi, Yuxi Lin, Masatomo So, Mihály Józsi, Gitta Schlosser, Young-Ho Lee, Károly Liliom, Yuji Goto, József Kardos
Pathogenic D76N Variant of β2-Microglobulin: Synergy of Diverse Effects in Both the Native and Amyloid States. Biology 10 (11) (2021)
Kichitaro Nakajima, Hajime Toda, Kei-Ichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto, Hirotsugu Ogi
Half-Time Heat Map Reveals Ultrasonic Effects on Morphology and Kinetics of Amyloidogenic Aggregation Reaction. ACS chemical neuroscience 12 (18) (2021)
Masatomo So, Yuto Kimura, Keiichi Yamaguchi, Toshihiko Sugiki, Toshimichi Fujiwara, Cesar Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Yasushi Kawata, Yuji Goto
Polyphenol-solubility alters amyloid fibril formation of α-synuclein. Protein science : a publication of the Protein Society 30 (8) (2021)
Masahiro Noji, Tatsushi Samejima, Keiichi Yamaguchi, Masatomo So, Keisuke Yuzu, Eri Chatani, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yasushi Kawata, Kensuke Ikenaka, Hideki Mochizuki, József Kardos, Daniel Erik Otzen, Vittorio Bellotti, Johannes Buchner, Yuji Goto
Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications biology 4 (1) (2021)
Maya Sawada, Kei-Ichi Yamaguchi, Miki Hirano, Masahiro Noji, Masatomo So, Daniel Erik Otzen, Yasushi Kawata, Yuji Goto
Amyloid Formation of α-Synuclein Based on the Solubility- and Supersaturation-Dependent Mechanism. Langmuir : the ACS journal of surfaces and colloids 36 (17) (2020)
Kichitaro Nakajima, Tomoya Yamazaki, Yuki Kimura, Masatomo So, Yuji Goto, Hirotsugu Ogi
Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals. The journal of physical chemistry letters 11 (15) (2020)
Kenji Sasahara, Kei-Ichi Yamaguchi, Masatomo So, Yuji Goto
Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation. The Journal of biological chemistry 294 (42) (2019)
Masahiro Noji, Kenji Sasahara, Kei-Ichi Yamaguchi, Masatomo So, Kazumasa Sakurai, József Kardos, Hironobu Naiki, Yuji Goto
Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH. The Journal of biological chemistry 294 (43) (2019)
Hiroya Muta, Masatomo So, Kazumasa Sakurai, Jozsef Kardos, Hironobu Naiki, Yuji Goto
Amyloid Formation under Complicated Conditions in Which β2-Microglobulin Coexists with Its Proteolytic Fragments. Biochemistry 58 (49) (2019)
Chun-Ming Zhang, Keiichi Yamaguchi, Masatomo So, Kenji Sasahara, Toru Ito, Suguru Yamamoto, Ichiei Narita, József Kardos, Hironobu Naiki, Yuji Goto
Possible mechanisms of polyphosphate-induced amyloid fibril formation of β2-microglobulin. Proceedings of the National Academy of Sciences of the United States of America 116 (26) (2019)
Masahiro Noji, Masatomo So, Kei-Ichi Yamaguchi, Hironobu Hojo, Maki Onda, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yuji Goto
Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization. Biochemistry 57 (37) (2018)
Masayuki Adachi, Masahiro Noji, Masatomo So, Kenji Sasahara, József Kardos, Hironobu Naiki, Yuji Goto
Aggregation-phase diagrams of β2-microglobulin reveal temperature and salt effects on competitive formation of amyloids versus amorphous aggregates. The Journal of biological chemistry 293 (38) (2018)