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Cold denaturation of α-synuclein amyloid fibrils.
Ikenoue T, Lee YH, Kardos J, Saiki M, Yagi H, Kawata Y, Goto Y. Ikenoue T, et al. Among authors: kawata y. Angew Chem Int Ed Engl. 2014 Jul 21;53(30):7799-804. doi: 10.1002/anie.201403815. Epub 2014 Jun 11. Angew Chem Int Ed Engl. 2014. PMID: 24920162
Breakdown of supersaturation barrier links protein folding to amyloid formation.
Noji M, Samejima T, Yamaguchi K, So M, Yuzu K, Chatani E, Akazawa-Ogawa Y, Hagihara Y, Kawata Y, Ikenaka K, Mochizuki H, Kardos J, Otzen DE, Bellotti V, Buchner J, Goto Y. Noji M, et al. Among authors: kawata y. Commun Biol. 2021 Jan 26;4(1):120. doi: 10.1038/s42003-020-01641-6. Commun Biol. 2021. PMID: 33500517 Free PMC article.
Polyphenol-solubility alters amyloid fibril formation of α-synuclein.
So M, Kimura Y, Yamaguchi K, Sugiki T, Fujiwara T, Aguirre C, Ikenaka K, Mochizuki H, Kawata Y, Goto Y. So M, et al. Among authors: kawata y. Protein Sci. 2021 Aug;30(8):1701-1713. doi: 10.1002/pro.4130. Epub 2021 Jun 2. Protein Sci. 2021. PMID: 34046949 Free PMC article.
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism.
Furukawa K, Aguirre C, So M, Sasahara K, Miyanoiri Y, Sakurai K, Yamaguchi K, Ikenaka K, Mochizuki H, Kardos J, Kawata Y, Goto Y. Furukawa K, et al. Among authors: kawata y. Curr Res Struct Biol. 2020 Apr 5;2:35-44. doi: 10.1016/j.crstbi.2020.03.001. eCollection 2020. Curr Res Struct Biol. 2020. PMID: 34235468 Free PMC article.
527 results