2023

2023.3.23
Keiichi Yamaguchi, Kichitaro Nakajima, Yuji Goto.
Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation
Biophysics and Physicobiology, 20,1 (2023)
[DOI:10.2142/biophysico.bppb-v20.0013]

2022

2022.10.3
Kichitaro Nakajima, Keiichi Yamaguchi, Masahiro Noji, César Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Lianjie Zhou, Hirotsugu Ogi, Toru Ito, Ichiei Narita, Fumitake Gejyo, Hironobu Naiki, Suguru Yamamoto and Yuji Goto.
Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis
nature communications, 13, 5689 (2022)
[DOI:10.1038/s41467-022-33247-3]
2022.7.21
Yuji Goto, Masahiro Noji, Kichitaro Nakajima and Keiichi Yamaguchi.
Supersaturation-Dependent Formation of Amyloid Fibrils
Molecules, 27(14), 4588 (2022)
[DOI:10.3390/molecules27144588]
2022.7.5
Yuki Yoshikawa, Keisuke Yuzu, Naoki Yamamoto, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Tetsushi Iwasaki, Masatomo So, Yuji Goto, Atsuo Tamura and Eri Chatani.
Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain
Molecules, 27(13),3964 (2022)
[DOI:10.3390/molecules27133964]
2022.7.5
Henrietta Vadászi, Bence Kiss, András Micsonai, Gitta Schlosser, Tamás Szaniszló, Réka Á.Kovács, Balázs A.Györffy, Katalin A.Kékesi1, Yuji Goto, Barbara Uzonyi, Károly Liliom and József Kardos.
Competitive inhibition of the classical complement pathway using exogenous single-chain C1q recognition proteins
Journal of Biological Chemistry, 298,7 (2022)
[DOI:10.1016/j.jbc.2022.102113]
2022.7.5
Kentaro Noi, Kichitaro Nakajima, Keiichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto and Hirotsugu Ogi.
Acceleration of amyloid fibril formation by multichannel sonochemical reactor
Japanese Journal of Applied Physics,61 (SG), SG1002 (2022)
[DOI:10.35848/1347-4065/ac4142]
2022.7.5
Makoto Hideshima, Yasuyoshi Kimura, César Aguirre, Keita Kakuda, Toshihide Takeuchi, Chi-Jing Choong, Junko Doi, Kei Nabekura, Keiichi Yamaguchi, Kichitaro Nakajima, Kousuke Baba, Seiichi Nagano, Yuji Goto, Yoshitaka Nagai, Hideki Mochizuki and Kensuke Ikenaka.
Two-step screening method to identify α-synuclein aggregation inhibitors for Parkinson’s disease
Scientific Reports,12(1),1-11 (2022)
[DOI:10.1038/s41598-021-04131-9]
2022.7.5
András Micsonai, Éva Moussong, Frank Wien, Eszter Boros, Henrietta Vadászi, Nikoletta Murvai, Young-Ho Lee, Tamás Molnár, Matthieu Réfrégiers, Yuji Goto, Ágnes Tantos, and József Kardos.
BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy
Nucleic Acids Research, (2022)
[hal-03670788]
2022.1.11
Yuji Goto , Kichitaro Nakajima, Keiichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, and Hirotsugu Ogi.
Development of HANABI, an ultrasonication-forced amyloid fibril inducer
Neurochemistry International,153, (2022)
[DOI:10.1016/j.neuint.2021.105270]

2021

2021.11.25
Masahiro Noji , Yuji Goto.
蛋白質フォールディングとミスフォールディングの統合
生物物理,61巻 6号,358-365 (2021)
[DOI:10.2142/biophys.61.358]
2021.11.17
Éva Bulyáki, Judit Kun, Tamás Molnár, Alexandra Papp, András Micsonai, Henrietta Vadászi, Borbála Márialigeti, Attila István Kovács, Gabriella Gellén, 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),1197 (2021)
[DOI:10.3390/biology10111197]
2021.10.7
Keiichi Yamaguchi, Kenshiro Hasuo, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, and Yuji Goto.
Strong acids induce amyloid fibril formation of β2-microglobulin via an anion-binding mechanism
Journal of Biological Chemistry,297,5 (2021)
[DOI:10.1016/j.jbc.2021.101286]
2021.9.1
Kichitaro Nakajima, Hajime Toda, Keiichi Yamaguchi, Masatomo So,Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto, and Hirotsugu Ogi.
Half-Time Heat Map Reveals Ultrasonic Effects on Morphology and Kinetics of Amyloidogenic Aggregation Reaction
ACS Chem. Neurosci.,12,18,3456-3466 (2021)
[DOI:10.1021/acschemneuro.1c00461]
2021.5.27
Masatomo So, Yuto Kimura, Keiichi Yamaguchi, Toshihiko Sugiki, Toshimichi Fujiwara, César Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Yasushi Kawata, and Yuji Goto.
Polyphenol-solubility alters amyloid fibril formation of α-synuclein
Protein Science,30(8),1701-1713 (2021)
[DOI:10.1002/pro.4130]
2021.4.21
Eri Chatani, Keisuke Yuzu, Yumiko Ohhashi, and Yuji Goto.
Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils
International Journal of Molecular Sciences, 22(9),4349 (2021)
[DOI:10.3390/ijms22094349]
2021.3.4
Keiichi Yamaguchi, Masatomo So, César Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Yasushi Kawata, and Yuji Goto.
Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners
Journal of Biological Chemistry, 296 (2021)
[DOI:10.1016/j.jbc.2021.100510]
2021.3.3
Kichitaro Nakajima, Kentaro Noi, Keiichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, Hirotsugu Ogi, and Yuji Goto.
Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation
Ultrasonics Sonochemistry, 73 (2021)
[DOI:10.1016/j.ultsonch.2021.105508]
2021.1.26
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 E. Otzen,Vittorio Bellotti, Johannes Buchner, and Yuji Goto.
Breakdown of supersaturation barrier links protein folding to amyloid formation
Communications Biology, 4 ,120 (2021)
[DOI:10.1038/s42003-020-01641-6]

2020

2020.05.05
Sawada M, Yamaguchi K, Hirano M, Noji M, So M, Otzen D, Kawata Y, and Goto Y.
Amyloid Formation of α-Synuclein Based on the Solubility- and Supersaturation-Dependent Mechanism
Langmuir, 36(17) , 4671-4681 (2020)
[PMID: 32271585]
2020.04.05
Furukawa K, Aguirre C,So M,Sasahara K,Miyanoiri Y,Sakurai K,Yamaguchi K,Ikenaka K,Mochizuki H,Kardos J,Kawata Y, and Goto Y.
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism
Curr Res Struct Biol, 2 , 35-44 (2020)
[DOI: 10.1016/j.crstbi.2020.03.001]
2020.02.11
Taricska N, Horvath D, Menyhard DK, Akontz-Kiss H, Noji M, So M, Goto Y, Fujiwara T, and Perczel A.
The route from the folded to the amyloid state: exploring the potential energy surface of a drug‐like miniprotein.
Chemistry, 26 , 1968-1978 (2020)
[PMID: 31647140]

2019

2019.12.10
Muta H, So M, Sakurai K, Kardos J, Naiki H, and Goto Y.
Amyloid Formation under Complicated Conditions in Which β 2-Microglobulin Coexists with Its Proteolytic Fragments
Biochemistry, 58 , 4925-4934 (2019)
[PMID: 31724398]
2019.10.25
Noji M, Sasahara K, Yamaguchi K, So M, Sakurai K, Kardos J, Naiki H, and Goto Y.
Heating during agitation of β 2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH
J Biol Chem, 294 , 15826-15835 (2019)
[PMID: 31495783]
2019.6.25
Zhang C, Yamaguchi K, So M, Sasahara K, Ito T, Yamamoto S, Narita I, Kardos J, Naiki H, and Goto Y.
Possible mechanisms of polyphosphate-induced amyloid fibril formation of β 2-microglobulin
Proc Natl Acad Sci U S A, 116 ,12833-12838 (2019)
[PMID: 31182591]
2019.4.12
Kakuda K, Ikenaka K, Araki K, So M, Aguirre C, Kajiyama Y, Konaka K, Noi K, Baba K, Tsuda H, Nagano S, Ohmichi T, Nagai Y, Tokuda T, El-Agnaf OMA, Ogi H, Goto Y, and Mochizuki H.
Ultrasonication-based rapid amplification of α-synuclein aggregates in cerebrospinal fluid.
Sci Rep, 9 ,6001 (2019)
[PMID: 309799351]