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pro vyhledávání: '"Naoya Fukui"'
Autor:
Yuxi Lin, Naoya Fukui, Mayu S. Terakawa, Toshihiko Sugiki, Yuji Goto, Young-Ho Lee, Yasushi Kawata, Misaki Kinoshita, Tatsuya Ikenoue
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860:757-766
Amyloid fibrillation causes serious neurodegenerative diseases and amyloidosis; however, the detailed mechanisms by which the structural states of precursor proteins in a lipid membrane-associated environment contribute to amyloidogenesis still remai
Autor:
Yasuharu Shinoda, Yasushi Yabuki, Yuki Aoyama, Naoya Fukui, Hanae Yamamoto, Kohji Fukunaga, Tomohiro Mizobata, Ichiro Kawahata, Yasushi Kawata, Kunihiro Hongo, Moe Miyabe
Publikováno v:
The Journal of Biological Chemistry
Fukui, Naoya. Yamamoto, Hanae. Miyabe, Moe. et al. An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3. Journal of Biological Chemistry. 296, 100663. 2021-04-20.
Fukui, Naoya. Yamamoto, Hanae. Miyabe, Moe. et al. An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3. Journal of Biological Chemistry. 296, 100663. 2021-04-20.
α-synuclein (αSyn) is a protein known to form intracellular aggregates during the manifestation of Parkinson’s disease. Previously, it was shown that αSyn aggregation was strongly suppressed in the midbrain region of mice that did not possess th
Publikováno v:
Ojha Bimlesh, Fukui Naoya, Hongo Kunihiro, et al. Suppression of amyloid fibrils using the GroEL apical domain. Scientific Reports. 2016. 6. doi:10.1038/srep31041
Scientific Reports
Scientific Reports
In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191–376), which r